New material for efficient separation of Deuterium at elevated Temperatures

New material for efficient separation of Deuterium at elevated Temperatures

A novel porous material capable of separating deuterium (D2) from hydrogen (H2) at a temperature of 120 K has been introduced. Notably, this temperature exceeds the liquefaction point of natural gas, thus facilitating large-scale industrial applications. This advancement presents an attractive pathway for the economical production of D2 by leveraging the existing infrastructure of liquefied natural gas (LNG) production pipelines. The research conducted by Ulsan National Institute of Science & Technology (UNIST), Korea, Helmholtz-Zentrum Berlin, Heinz Maier Leibnitz Zentrum (MLZ), and Soongsil University, Korea, has been published in Nature Communications.

Deuterium, a stable isotope of hydrogen, plays a critical role in enhancing the durability and luminous efficiency of semiconductors and display devices, as well as serving as a fusion fuel in energy production. However, the increasing demand for D2 presents challenges in its production, primarily due to the need to separate from hydrogen through a cryogenic distillation process conducted at temperatures as low as 20 K (-253°C). While research has explored the use of metal-organic frameworks (MOFs) for D2 separation, their efficiency diminishes significantly at elevated temperatures.

In this study, the research team presented a copper-based zeolite imidazolate framework (Cu-ZIF-gis), which shows exceptional D2 separation performance, even at 120 K (-153℃). While typical MOFs operate effectively at around 23 K (-250℃), their performance decreases sharply as temperatures approach 77 K (-196℃). However, the newly developed Cu-based MOF demonstrates a significant advantage in maintaining its effectiveness at higher temperatures.

For the first time, the research team identified that the superior performance of this material results from the increased expansion of its lattice as the temperature rises. At cryogenic temperatures, the pores of the developed MOF are smaller than H2 molecules, thereby inhibiting their passage. However, as the temperature increases, the lattice expands, leading to an increase in pore size. This enlargement facilitates the passage of gases through the pores, thereby enabling the separation of H2 and D2 via the quantum sieving effect, wherein heavier molecules traverse the pores more efficiently at lower temperatures.

Confirmatory in-situ X-ray diffraction (XRD) and quasi-elastic neutron scattering (QENS) experiments, conducted at the Institut Laue-Langevin (ILL) in Grenoble, France, by the joint team from UNIST, HZB and MLZ, confirmed the expansion of the lattice framework with increasing temperature, as well as the difference in isotope diffusivity even at elevated temperatures. Additionally, the analysis from the Thermal Desorption Spectroscopy (TDS) experiments indicated stable D2 separation at elevated temperatures.

Read more on HZB website

Image: The crystal structure of Cu-ZIF-gis that shows cylindrical straight channels along the c-axis. The pores were calculated with Connolly surfaces with a probe of 1.1 Å. (Cu, orange; N, blue; C, gray; O, magenta; H, white).

Credit: Minji Jung / Department of Chemistry, UNIST

Non-destructive study of ancient glass and other vitreous materials from Southwest Asia

Non-destructive study of ancient glass and other vitreous materials from Southwest Asia

The availability of a SXCT (Synchrotron X-ray Computed Tomography) facility at the heart of Southwest Asia facilitates and enhances the non-destructive examination and conservation of ancient vitreous materials of the region, proving the relevance of the technique for archaeologists, museums, and cultural heritage specialists.

In recent measurements at SESAME’s ID10-BEATS beamline, users from Italy, Jordan, Palestine, Switzerland and Türkiye joined SESAME’s beamline scientists, Gianluca Iori, Latif Ullah Khan and Philipp Hans, in the application of Synchrotron X-ray Computed Tomography (SXCT) for the non-destructive analysis of ancient glass, faience, and several other vitreous materials. The results of their work have been published in the Journal of Cultural Heritage 

The international and multidisciplinary composition of this team demonstrates not only the wide-ranging applications of synchrotron techniques, but also the collaborative spirit fostered by the Facility. This highlights how SXCT serves as a versatile tool for cultural heritage research across different geographical and academic contexts, and shows its potential to address varied scientific and conservation challenges. 

The analysis of archaeological objects poses a set of challenges arising from the fragility and uniqueness of the materials, and requires special non-invasive techniques.

SXCT brings the solution to this as it provides high-resolution 3D X-ray images which, with no invasive techniques likely to damage the objects, permits the understanding of the structure and chemical composition of ancient artifacts. It also reveals details not detectable by conventional techniques.

Thanks to SXCT, researchers are able to examine fragile artifacts, and so understand how they were produced. It also provides information on their aging process, and how they are to be conserved for future generations, and this irrespective of the size of the objects.

Read more on SESAME website

Image: Detector Hasselblad lenses (1x magnification) with ORYS FLIR camera; 4.5 micron voxel size

Credit: SESAME

Targeted Destruction of Disease-Related Proteins

Targeted Destruction of Disease-Related Proteins

A new protein construct helps scientists study drugs that break down protein targets.

While most conventional drugs work by inhibiting proteins, not all proteins are easy to block in this fashion. Drug developers are investigating new classes of drugs that mark proteins for degradation in the cell. A large, barrel-shaped structure called the proteasome drives this breakdown process, and a protein called Cereblon behaves as an usher, delivering proteins to the proteasome for destruction. Some drugs act as “molecular glue”, sticking to Cereblon and altering its structure so that it binds to target proteins. Other drugs called proteolysis targeting chimeras (PROTACs) bind to target proteins and Cereblon, bridging the two together. Thus, an in-depth understanding of Cereblon’s morphology is crucial for drug investigations. However, scientists have struggled to determine high-resolution structures of this protein in the past due to complications with its synthesis and stability. David Zollman, a structural biologist and drug developer at the University of Dundee, and his colleagues developed a highly stable, easily purified Cereblon variant. Collecting X-ray crystallography data at the Diamond Light Source beamlines I04 and I24, they demonstrated that the structure of their Cereblon variant matched ones previously collected by other groups, but the new crystals achieved higher resolution. Cereblon changes shape when bound to different drugs, and the team collected small-angle X-ray scattering (SAXS) data at beamline B21 to study how shapeshifting varies between different drug candidates. Together, these findings reveal that the new Cereblon variant is amenable to structural analysis, which could facilitate future research into this promising class of protein-degrading drugs. 

Most conventional drugs work by inhibiting proteins. The pain-reliever ibuprofen, for example, blocks a bodily enzyme called cyclooxygenase by stoppering its active site and preventing it from producing chemical signals that induce pain. However, Zollman said that researchers have long considered some proteins “undruggable” because they lack active sites that can be targeted by inhibitors. These include proteins that have structural roles rather than enzymatic functions. Taking an alternative approach, scientists are exploring drugs that flag proteins for degradation in the cell by protein shredders called proteasomes. 

The most infamous example is the drug thalidomide, a sedative from the 1950s that pregnant women took to relieve morning sickness but led to birth defects. Today, doctors have repurposed thalidomide to treat multiple myeloma, and researchers have developed other drug candidates, like lenalidomide and mezigdomide to treat other cancers. Currently, there are over 40 drugs related to the degradation pathway in cells undergoing clinical trials. Many of them work by recruiting transcription factors to Cereblon and targeting them for destruction, thereby preventing the expression of an array of genes.  

Research into these drugs has been held back by a lack of structural insight into Cereblon. Previously, scientists could only purify Cereblon coupled with an adapter protein called Damage Specific DNA Binding Protein 1 (DDB1), resulting in an unwieldy complex. Scientists also struggled to produce high yields of the protein, and they could only prepare it in insect cell expression systems. When scientists managed to crystallize the protein, they found it was unstable, hampering efforts to collect high-resolution structural data. Most experiments determined the structure to a resolution of 3 Ångströms (Å) or worse. Dr Zollman said:

It’s expensive to produce, hard to get in large quantities, and then when you do have it, it’s quite poorly behaved.

What scientists needed was a stable version of Cereblon that was easy to purify in the absence of DDB1. Dr Zollman commented:

We have cut out the part of Cereblon that binds to DDB1, and because of that, we are able to produce it stably from E. coli on its own.

E. coli are the go-to bacteria for producing proteins for purification, making it easier to achieve high yields for scientific studies. 

Besides omitting the DDB1-binding domain, Zollman’s team designed 15 versions of Cereblon, some of which carried unique sets of mutations that swap out one amino acid for another in different places. They introduced these mutations to stabilize the proteins, and they discovered that version 8, complete with 12 mutations, proved most stable. “We can get it at a much higher yield, it’s much cheaper to produce, it’s much easier to produce, and then the complex does crystallize a lot better.” Zollman said version 8 is a “middle ground” between full-length Cereblon and other truncated versions trialled previously, so his team renamed it Cereblonmidi.  

Next, they had to put their crystallised Cereblonmidi to the test at the Diamond Light Source. Zollman said the protein formed small crystals, and the microfocus beams at beamlines I04 and I24 enabled his team to collect high-quality data from samples of this size. 

Read more on Diamond website

A Goldilocks promoter for a silver catalyst

A Goldilocks promoter for a silver catalyst

Nickel dopants could improve sustainable production of ethylene oxide, a chemical widely used in industrial manufacturing.

Plastics, textiles, detergents, adhesives and antifreeze all have something in common: They were made using ethylene oxide. This colorless gas, a chemical building block in the industrial production of many materials, is itself produced by reacting oxygen with ethylene. However, maximizing the amount of ethylene oxide produced poses unique challenges. 

Adding chlorine increases the efficiency of ethylene oxide production by 25 percent. But chlorine, which is corrosive to metal equipment, has its own drawbacks. Writing in Science, researchers at the University of California, Santa Barbara (UCSB), Tufts University, Brookhaven National Laboratory and Tulane University identified nickel as a promoter that can enhance the selectivity of the silver catalyst by about 25 percent, roughly the same amount as chlorine, but with fewer downsides. The team studied the interaction of nickel with the silver catalyst using X-rays from the Stanford Synchrotron Radiation Lightsource (SSRL) at the Department of Energy’s SLAC National Accelerator Laboratory. 

“From an environmental standpoint, if you remove chlorine, that’s one less toxic and corrosive material out of the process stream,” said Adam Hoffman, a staff scientist at SLAC who contributed to this work. “And if you can improve a catalyst’s activity to a target chemical, it improves the sustainability of the process as a whole.”

Charles Sykes, a chemist at Tufts University who led the effort, said it also makes financial sense. “Every one percent increase in the efficiency of the process saves around $200 million annually,” he said.

If you remove chlorine, that’s one less toxic and corrosive material out of the process stream.

Adam Hoffman SLAC Staff Scientist

A more selective catalyst doesn’t only maximize the amount of product, it is also more efficient overall. Post reaction, ethylene oxide must be separated from the side products and residual reactants, a process that requires additional energy inputs. If the reaction is more selective to ethylene oxide to begin with, it is easier to purify.

Read more on SLAC website

Image: A computer-generated image showing single nickel (Ni) atoms embedded in silver, used to enable efficient production of ethylene oxide. 

Credit: Elizabeth Happel/Tufts University

Scientists find ways to reduce oil intake in deep fried foods

Scientists find ways to reduce oil intake in deep fried foods

A new 4D imaging system has tracked the process of frying foods at the ESRF, in a quest to make the products absorb less oil and therefore, healthier. Their insights show that it is especially after frying, during the cooling process, that food absorbs oil, and that the amount of oil absorbed depends on the porous structure created during frying. The results are out in Nature Communications.

Fried foods are staple especially in Western diets due to their distinct flavour and sensory characteristics. The frying process causes foods to develop unique textures related to their crispy outside and soft inside.

“People like fried products because of the texture and the taste, but they have been claimed to be an ultra-processed food that we should try to minimise in our diet”, explains Pieter Verboven of KU Leuven in Belgium, corresponding author of the publication. “Still, the final composition is more of a concern than the process itself”, he adds. Therefore, the KU Leuven research team are investigating ways to reduce oil content but preserve texture and taste.

When we fry food, we submerge it into hot oil that is more than 160 °C. This leads to very fast evaporation of water and creates internal pressure in the form of steam, which results in an expanding porous structure. “This process is extremely fast, in the order of seconds, and we don’t have the tools to see what happens in real-time, so we need to come to the ESRF to be able to track the process”, says Verboven.

A fryer on the beamline

The team came to ID19 to carry out high-speed 4D computed tomography on wheat flour dough, a common food material subjected to deep-frying. The experiments took place as the dough was frying in a custom oil fryer and afterwards, during the post-frying cooling, with the aim of investigating the structural deformation and pore formation, as well as oil uptake. “The experiment was extremely complex, as we needed to scan the sample submerged in oil very fast to track all the changes at the microstructural level”, explains Bratislav Lukic, researcher at the ESRF and co-author of the publication, “The fryer was also equipped with sensors and actuators to precisely control the process remotely. Thanks to high flux at high energy of the Extremely Brilliant Source, we were able to reach sub-second scanning times while maintaining microscopic spatial resolution, all that in a very large fryer, which is representative of the process.”

They visualised how the product expands due to steam during the frying process, which hinders the oil from getting inside. At the same time, the physico-chemical changes in starch and gluten structure determine the pore structure. The trick is to control this process well to create the desired texture with a crispy crust and fluffy interior. The team found that oil is absorbed mostly during the cooling of the fried dough and, in smaller percentage, during the frying process itself.

Read more on ESRF website

Analyzing Metal Interface Reactions in All-Solid-State Batteries

Analyzing Metal Interface Reactions in All-Solid-State Batteries

This study developed a real-time X-ray photoelectron spectroscopy (XPS) analysis technique and utilized it to understand the lithium-ion behavior at metal interface layers in all-solid-state secondary batteries. Notably, the result of this research was published as a cover article in Advanced Energy Materials, one of the leading journals in the field, highlighting its significance.

Research Background and Goals
All-solid-state batteries (ASSBs) are gaining attention as next-generation batteries, offering higher energy density and enhanced safety than conventional liquid lithium-ion batteries (LIBs). In particular, lithium lanthanum zirconium oxide (LLZO)-based electrolytes are considered a key material for next-generation batteries because they exhibit excellent properties, including high ionic conductivity, chemical stability, and a wide bandgap. However, to ensure the long-term stability of batteries, it is necessary to understand their role at metal interfaces (Au, Ag) within the battery. Conventional XPS analyses have the strength of accurately measuring chemical property changes. However, they have limitations in analyzing under real conditions, as lithium compounds can be degraded due to their high reactivity in air during batteries’ charge-discharge. To solve this problem, the research team developed a real-time XPS analysis technique that can compare the reactions of Au and Ag metal interfaces with the previous analyses to elucidate the lithium-metal interaction mechanisms.

Methods
The research team performed real-time charge-discharge analysis using Ag and Au battery cells deposited onto the interface layers between LLZO solid electrolytes and current collectors. Then, Li-ion behavior was analyzed for high spatial resolution using operando XPS and scanning photoelectron microscopy (SPEM). This analysis was used to examine the spatial distribution of Li ions at a high resolution. These methods provided deeper insights into Li-ion migration mechanisms.

Results and Discussion
This study optimized a reliable real-time (operando) XPS analysis technique to determine the factors determining the ASSB performance. While conventional analysis methods are limited in making real-time observations of material changes at metal interfaces during the charge-discharge process, the newly developed real-time XPS technique enables analyzing the precise chemical and electronic structures of metal interface layers at each stage. The research team thoroughly examined the impact of metal interface layers, such as Ag, Au, and Cu, on the ASSB interfacial properties through this approach. As a result, it was confirmed that an increase or decrease in Li⁰ content serves as a critical metric for assessing the efficiency and reversibility of Li plating/stripping processes. Additionally, this research discovered that oxygen bonding within the metal interface layers reacts with Li⁺ ions to form Li₂O, which influences the chemical stability of interfaces. Furthermore, while comparative analysis of core-level electrons showed no significant changes, the formation of Li-metal alloys could be judged by changes in valence-band structure. Based on these analyses, this research identified the key factors that make Ag interface layers superior to other metal interface layers in terms of interface stability and ASSB performance.

Read more on PAL website

Synchrotron light opens new avenues for aquaculture disease prevention

Synchrotron light opens new avenues for aquaculture disease prevention

A collaborative study by the Institute for Research, Development, and Innovation in Health Biotechnology of Elche (IDiBE) and the ALBA Synchrotron has used cryo-soft X-ray tomography to investigate the viral response of rainbow trout red blood cells (RBCs) to the virus commonly known as ‘fish Ebola’.

The research, published in Frontiers in Immunology, reveals significant cellular structural changes that could inform novel fish vaccine development, a critical need in aquaculture.

Fish nucleated red blood cells, also known as erythrocytes, play a crucial role in maintaining immune system balance in response to various stimuli, including viral attacks. Previous studies have shown that erythrocytes undergo intracellular changes – such as endoplasmic reticulum (ER) stress, autophagy, and antigen presentation – to prevent viral replication in response to viruses and DNA vaccines. A deeper understanding of this response could aid the development of new preventive treatments, particularly much-needed vaccines for the aquaculture industry.

To investigate these mechanisms, researchers from Institute for Research, Development and Innovation in Health Biotechnology of Elche (IDiBE) of the Miguel Hernández University (UMH) and the MISTRAL beamline at ALBA Synchrotron studied the response of rainbow trout erythrocytes when exposed to viral hemorrhagic septicemia virus (VHSV). This highly contagious virus severely affects various fish species, with mortality rates of up to 100%. For this reason, it has been commonly referred to as “fish Ebola.“

To examine in detail the erythrocytes’ response, researchers employed advanced imaging techniques at the ALBA Synchrotron. Cryo-soft X-ray tomography (cryo-SXT) – available in five places all over the world, being one of them the MISTRAL beamline – is a novel approach that enables the visualization of 3D nanoscale structures in intact cryopreserved cells.

The research team purified rainbow trout erythrocytes and exposed them to VHSV. At the ALBA Synchrotron, they visualized the structural differences in infected cells, revealing that rainbow trout erythrocytes experience an increase of the endoplasmic reticulum volume and activate the endoplasmic reticulum stress process. Using molecular biology techniques, the team verified that this process activates the misfolded protein response (UPR). The UPR is an internal defence mechanism that cells trigger when faced with stress. Furthermore, by inhibiting reticulum stress, they discovered that the virus increased its replication, demonstrating that this process contributes to slowing the infection.

The results suggest that rainbow trout erythrocytes modulate endoplasmic reticulum stress as an antiviral control mechanism and open a new line of research to identify antiviral strategies targeting erythrocytes.

Read more on ALBA website

Image: General picture of rainbow trouts. Image obtained by soft X-ray cryotomography at the MISTRAL beamline at the ALBA Synchrotron. 3D image of erythrocytes exposed to VHSV, showing the cell nucleus in pink, the endoplasmic reticulum in yellow, the cytoplasm in green, and double-membrane vesicles in purple.

ANSTO scientists help refine estimates of global methane emissions

ANSTO scientists help refine estimates of global methane emissions

A groundbreaking international study published in the Journal of Geophysical Research: Atmospheres has provided new insights into global fossil methane emissions, using innovative multi-isotopic atmospheric measurements.  

Principal Accelerator Scientist Dr Andrew Smith, a co-author who has investigated methane emissions for over two decades with A/Prof Vasilii Petrenko and others, contributed significantly to this collaborative research, which has improved the accuracy of greenhouse gas emission estimates and support more effective global climate mitigation efforts. 
 

The study, led by Dr Ryo Fujita of the Imperial College London and the Japanese Meteorological Research Institute in Tsukuba, used advanced isotopic analysis, including radiocarbon and stable isotopes of carbon and hydrogen, to accurately distinguish between different methane emission sources. This research is the first research to integrate multiple isotopic datasets to precisely quantify global methane emissions from fossil fuels, biogenic, geologic, and biomass burning sources across the historical timeframe from 1750 to 2015. 

One key finding of the study was that global fossil methane emissions are about 130 teragrams per year for the period 2003–2012, which closely matches the Global Carbon Project estimates, a network of scientists and institutions investigating greenhouse gases. To put this into perspective, a teragram is one trillion grams, approximately equivalent to the mass of water in 400 Olympic-sized swimming pools.  
 

Importantly, the study contradicts earlier claims of significantly underestimated fossil methane emissions, bringing clarity to previously conflicting scientific assessments. 

Dr. Smith highlighted the importance of multi-isotopic measurements for resolving uncertainties in methane emission inventories. “This study demonstrates that combining multiple isotopic constraints significantly reduces uncertainties in methane emission estimates. Such precise data are crucial for effective climate policy and mitigation strategies,” he said. 

ANSTO’s Centre for Accelerator Science, a world leader in extracting and accurately measuring radiocarbon from minuscule carbon samples.  This intricate process requires the identification and counting of individual atoms through accelerator mass spectrometry.  

Read more on ANSTO website

Dynamic protein nanotubes for advanced applications

Dynamic protein nanotubes for advanced applications

A collaborative research team from Jagiellonian University in Poland and the universities of Leeds, York, and Durham in the UK have made a significant nanotech breakthrough by developing dynamic, pentamer-based protein nanotubes. The study, published in ACS Nano, reveals how an engineered enzyme can assemble into various hollow spherical and cylindrical structures in response to stimuli.

By leveraging the power of electron microscopy and mathematical modeling, the research led by the Azuma group at Malopolska Centre of Biotechnology (MCB) JU has unlocked the ability of a modified enzyme, called lumazine synthase, to form versatile and adaptive nanostructures. The protein shows an extraordinary capacity to morph between hollow spherical shapes and elongated, fiber-like nanotubes, all in response to salt contents in solution. Unlike conventional nanotubes that rely on hexameric or other subunit arrangements, these newly discovered assemblies consist entirely of pentamers. 
Thanks to the state-of-the-art Titan Krios G3i cryo-electron microscope, housed at the National Synchrotron Radiation Centre SOLARIS JU and the Polish high-performance computing infrastructure PLGrid (HPC Centers: ACK Cyfronet AGH), scientists have mapped the structures of these innovative nanocage complexes with remarkable precision.

This pioneering research provides invaluable insights into the molecular mechanics and geometric principles of protein assembly. The findings offer a fresh blueprint for designing nanoarchitectures with customizable shapes and functions, potentially revolutionizing fields such as drug delivery, catalysis, and the creation of advanced nanomaterials.

This discovery is thrilling, as it allows us to see and comprehend the various ways pentamers bind within these nanocages – says Dr. Łukasz Koziej, a leading researcher of the study.
Dr. Yusuke Azuma adds, This work is a promising step forward to pave the way for developing new biomimetic devices and materials with bespoke properties, marking a significant advancement in the field of nanotechnology.

Read more on SOLARIS website


Image: Electron microscopic structures of ball- and tube-shaped assemblies made from an engineered enzyme, lumazine synthase. Unlike many other cases found before, these structures are built entirely with pentameric (pentagonal) units. By simply changing the amount of salt in the solution, they can switch between forming balls or tubes.

Breaking boundaries in biomedicine: APS enables protein design

Breaking boundaries in biomedicine: APS enables protein design

From growth hormones to cancer drugs, small molecules play a crucial role in our health. Monitoring them is essential to keeping us healthy; it enables physicians to calculate dosages and patients to monitor their medical conditions at home, for example.

Monitoring small molecules depends on sensing where they are, and in what concentrations. While scientists have developed sensors to detect some small molecules, these sensors are used primarily in research and drug discovery and can only detect a limited range of molecules with particular qualities. There is a compelling need for sensors that can detect and signal the presence of diverse small molecules of different shapes, sizes, flexibility and polarity. 

Using artificial intelligence (AI), a team of scientists led by Nobel Prize winner David Baker at the University of Washington has created a computational method for generating proteins that bind and signal a wide range of small molecules with great effectiveness. Baker won the 2024 Nobel Prize in Chemistry for computational protein design.

The research described here, published in Science and conducted in part at the Advanced Photon Source (APS), exemplifies that approach. The APS is a U.S. Department of Energy (DOE) Office of Science user facility at DOE’s Argonne National Laboratory.

The sensor design problem

Creating a protein sensor for small molecules is very difficult. The protein must first bind to the small molecule, then signal its presence. 

The team solved both problems with modular design strategies. Their AI-generated proteins consist of identical repeating subunits surrounding a central cavity. The cavity holds a pocket where the small molecule binds.

The subunits, being modular, are easily disassembled. In this way, the small molecule binding proteins can be treated like Lego blocks and be connected to well-established signaling proteins (such as split green fluorescent protein, or GFP), to make a full sensing protein device. When a small molecule binds in the pocket, the subunits reassemble, which leads to the signaling module sending a signal that the small molecule is present.

First step: Binding

The team chose a diverse spectrum of ligands (molecules that bind to protein receptors to send signals between cells), including cholic acid, a biomarker for liver disease; methotrexate, a cancer drug, which requires regular monitoring; thyroxine, a human hormone that indicates thyroid conditions; and a cyclic peptide.

The scientists constructed a machine learning algorithm based on AlphaFold2 (a protein structure predictor whose developers, John Jumper and Demis Hassabis, shared the Nobel Prize in Chemistry with Baker) and other machine learning protein design algorithms to generate thousands of proteins to bind the small molecules.

After computational design, the team tested the designed proteins in the laboratory and identified binders to particular ligands, following computational design and using machine learning methods to choose the best designs for experimental tests.

To confirm the accuracy of their design approach, the Baker team turned to the APS. They used the ultrabright X-ray beams to collect data on the atomic structure of the binding proteins. Using the Northeastern Collaborative Access Team (NE-CAT) beamlines at 24-ID at the APS, the team determined the structures of crystals formed from one of the designed proteins. 

“Prediction algorithms are excellent tools, but without verification of the structures, there’s no proof that the predictions match reality,” said Kay Perry of Cornell University, staff scientist at NE-CAT. ​“X-ray crystallography remains one of the best ways to make that confirmation, and the team was able to do so in this case.”

Second step: Signaling

The next challenge was turning the binding proteins into signaling proteins. The scientists took advantage of their modularity to create two different types of signaling events. 

The team built ligand-induced dimerization proteins from the binders. Linna An, the first author of this study, said the technology can be used in many health-related applications, such as regulating the release of drugs in cancer therapies.

In a different type of signaling event, the scientists fused the binding proteins to a newly designed nanopore, a protein creating a channel allowing ion flow. The fused unit was constructed in such a way that when a small molecule blocked the binding pocket, the whole nanopore was blocked, preventing the flow of ions and loss of current. Loss of current signaled the presence of the small molecule. 

Read more on APS website

Image: The crystal structure of CHD_r1 (gray) is very similar to the computational design model (colored).

Credit: Linna An, et al., Science.

X-ray snapshot: How light bends an active substance

X-ray snapshot: How light bends an active substance

With the help of the world’s most powerful X-ray laser, European XFEL, a research team led by Goethe University Frankfurt and the research centre DESY has achieved an important breakthrough: Using the example of the pharmaceutically active substance 2-thiouracil, they applied a long-established imaging technique to complex molecules for the first time. Although 2-thiouracil is no longer applied therapeutically, it is part of a group of chemically similar active substances that are used today as immunosuppressants or cytostatics. The study shows how UV radiation deforms 2-thiouracil, making it dangerously reactive.

Many biologically important molecules change shape when stimulated by UV radiation. Although this property can also be found in some drugs, it is not yet well understood. Using an innovative technique, an international team involving researchers from Goethe University Frankfurt, the European XFEL in Schenefeld and the Deutschen Elektronen-Synchrotron DESY in Hamburg has elucidated this ultra-fast process, and made it visible in slow motion, with the help of X-ray light. The method opens up exciting new ways of analysing many other molecules.

“We investigated the molecule 2-thiouracil, which belongs to a group of pharmaceutically active substances based on certain DNA building blocks, the nucleobases,” says the study’s last author Markus Gühr, the head of DESY’s free-electron laser FLASH and Professor of Chemistry at University of Hamburg. 2-thiouracil and its chemically related active substances have a sulphur atom, which gives the molecules its unusual, medically relevant properties. “Another special feature is that these molecules become dangerously reactive when exposed to UV radiation.” Studies indicate an increased risk of skin cancer due to this effect.

To better understand what happens during such processes, the research team used an already well-established method, bringing it to a new level by applying the technical possibilities available today. “Coulomb explosion imaging involves irradiating a molecule with intense X-ray pulses, which knock out electrons,” explains Till Jahnke, Professor of Experimental Atomic and Molecular Physics at Goethe University and the study’s first author. “Thereby, the molecule charges up positively and thus becomes unstable, so that it is torn apart within fractions of a second.” By tracking the direction in which the various fragments of the molecule – the atoms – fly apart, it is possible to derive information about the molecule’s structure. 

Read more on European XFEL website

Image: The SQS instrument’s COLTRIMS reaction microscope was used to analyze the structural changes of the 2-thiouracil molecule at the European XFEL.

Credit: European XFEL

A New Way to Engineer Composite Materials

A New Way to Engineer Composite Materials

  • Researchers have developed a way to engineer pseudo-bonds in a polymer material.
  • Their work represents a new way of solidifying materials without relying on permanent chemical bonds.
  • Like an epoxy, the material serves as a strong and stable filler—but can also be dissolved and reused, as though untangling a ball of yarn.

Composite adhesives like epoxy resins are excellent tools for joining and filling materials including wood, metal, and concrete. But there’s one problem: once a composite sets, it’s there forever. Now there’s a better way. Researchers have developed a simple polymer that serves as a strong and stable filler that can later be dissolved. It works like a tangled ball of yarn that, when pulled, unravels into separate fibers.

A new study led by researchers at the Department of Energy’s Lawrence Berkeley National Laboratory (Berkeley Lab) outlines a way to engineer pseudo-bonds in materials. Instead of forming chemical bonds, which is what makes epoxies and other composites so tough, the chains of molecules entangle in a way that is fully reversible. The research is published in the journal Advanced Materials.

“This is a brand new way of solidifying materials. We open a new path to composites that doesn’t go with the traditional ways,” said Ting Xu, a faculty senior scientist at Berkeley Lab and one of the lead authors for the study.

Read more on the Lawrence Berkeley National Lab website

Image: Silica nanoparticles affixed with a distribution of polystyrene chains (purple) self-assemble into hexagonal lattices. Depending on how the chains are organized on the particle surface, they tangle together (purple) or unravel (blue) when compressed. 

Credit: Tiffany Chen; Ting Xu

“Vortion”, a new magnetic state able to mimic neuronal synapses

“Vortion”, a new magnetic state able to mimic neuronal synapses

Researchers from the Universitat Autònoma de Barcelona (UAB) have managed to experimentally develop a new magnetic state: a magneto-ionic vortex or “vortion”. The research, published in Nature Communications, allows for an unprecedented level of control of magnetic properties at the nanoscale and at room temperature, and opens new horizons for the development of advanced magnetic devices. Controlling this state paves the way for the creation of more intelligent, reconfigurable and energy-efficient devices that mimic the brain.

The use of Big Data has multiplied the energy demand in information technologies. Generally, to store information, systems utilize electric currents to write data, which dissipates power by heating the devices. Controlling magnetic memories with voltage, instead of electric currents, can minimise this energy expenditure. One way to achieve this is by using magneto-ionic materials, which allow for the manipulation of their magnetic properties by adding or removing ions through changes in the polarity of the applied voltage.

So far, most studies in this area have focused on continuous films, rather than on controlling properties at the nanometric scale in discrete “bits”, essential for high-density data storage. Moreover, it is known that new magnetic phenomena can emerge at the sub-micrometre scale, that do not exist at the macroscopic level, such as magnetic vortices – small swirl-like magnetic structures. These vortices have applications in the way magnetic data are currently recorded and read, as well as in biomedicine. Nevertheless, changing the vortex state in already prepared materials is often impossible or requires large amounts of energy.

Researchers from the UAB Department of Physics, in collaboration with scientists from the ICMAB-CSIC, the ALBA Synchrotron and research institutions in Italy and the United States, propose a new solution that combines magneto-ionics and magnetic vortices. Researchers experimentally developed a new magnetic state that they have named magneto-ionic vortex, or “vortion”. This new object allows “on-demand” control of the magnetic properties of a nanodot (a dot of nanometric dimensions) with high precision. This is achieved by extracting nitrogen ions through the application of voltage, thus allowing for efficient control with very low energy consumption.

Measurements at the ALBA Synchrotron were carried out at the CIRCE-PEEM beamline, whose technique provides an excellent method to confirm the envisaged spin configurations of the vortion state.

“This is a so far unexplored object at the nanoscale. There is a great demand for controlling magnetic states at the nanoscale but, surprisingly, most of the research in magneto-ionics has so far focused on the study of films of continuous materials. If we look at the effects of ion displacement in discrete structures of nanometre dimensions, the ‘nanodots’ we have analysed, we see that very interesting dynamically evolving spin configurations appear, which are unique to these types of structures”. Jordi Sort, ICREA researcher in the UAB Department of Physics and director of the research.

These spin configurations and the magnetic properties of the vortices vary as a function of the duration of the applied voltage. Thus, different magnetic states (e.g., vortices with different properties or states with uniform magnetic orientation) can be generated from nanodots of an initially non-magnetic material by the gradual extraction of ions through the application of voltage.

“With the ‘vortions’ we developed, we can have unprecedented control of magnetic properties such as magnetisation, coercivity, remanence, anisotropy or the critical fields at which vortions are formed or annihilated. These are fundamental properties for storing information in magnetic memories, which we are now able to control and tune in an analogue and reversible manner by a voltage-activated process with very low energy consumption. The voltage actuation procedure, instead of using electric current, prevents heating in devices such as laptops, servers and data centres, and it drastically reduces energy loss.” Irena Spasojević, postdoctoral researcher in the UAB Department of Physics and first author of the paper.

Researchers have shown that by precisely controlling the thickness of the voltage-generated magnetic layer, the magnetic state of the material can be varied at will, in a controlled and reversible manner, between a non-magnetic state, a state with a uniform magnetic orientation (such as that found in a magnet), and the new magneto-ionic vortex state.

Read more on ALBA website

Image: Jordi Sort and Irena Spasojević at the UAB, next to the Magneto-Optical Kerr Effect (MOKE) magnetometer that was used for in-situ measurements described in the work.

The brilliant art amongst our stars

The brilliant art amongst our stars

On 15 January 2025, the SpaceX Falcon 9 rocket launched from NASA’s Cape Canaveral Space Force Station in Florida bound for the Mare Crisium basin of the moon—carrying with it 47 artistic creations, including MAX IV colleague Filip Persson’s artwork, ‘MAX IV Control System’. The art will be part of humanity’s galactic impression to live for millions of years.

According to Persson, his artwork represents a new genre of art with requirements yet to be defined. “The idea with the genre ‘Technical Art’ is that a sufficiently complex machine can create art by being run in normal operation. So, no deliberate special run in order to create the art. It can, for example, be instabilities or other things creating a beautiful pattern.”

The work, curated for the MoonMars Museum project, was created with Python and Gephi software. All devices of the full control system of MAX IV along with all interconnections were extracted as a huge table. The table was then imported into Gephi as a node network and evolved using gravitational parameters, creating beautiful patterns resembling galaxies—a bit like a Big Bang but with the very different behaviour that all information about the control system and the connections remain intact.

“I have over the years seen a lot of beautiful graphs at MAX IV and I thought quite early, due to having a somewhat artistic mind, that it would be fun to do something with these images,” explained Filip Persson, who is MAX IV’s Assistant Head of Accelerator Operations.

The artworks are packaged both digitally, on a very resilient memory card, and analogue as laser etched into a nickel plate using state-of-the-art Nanofiche technology with 300 000 DPI resolution. The art is part of the company LifeShip’s payload called ‘Pyramid on the Moon’.

How does one define technical art? The parameters are something that Persson aims to classify so that more people from around the world can contribute to the genre.

Read more on MAXIV website

Catching light-activated proteins in action

Catching light-activated proteins in action

Light is an important feature of the natural world. Many organisms have developed sophisticated systems to detect light and then convey signals to sensory systems that respond. This can be achieved through coupled systems that contain both a light-sensing chromophore and a protein that passes on the information via protein conformational changes to other domains or proteins in the system.

However, these reactions work on very fast timescales and not much is known about the structural intermediates that are involved. This information is important for understanding how these systems work and could be useful for applications such as the design of light-activated cellular sensors for research or medical treatments.

In a recent publication, a collaborative team from the Korean Advanced Institute of Science and Technology (KAIST), the Korean Center for Advanced Reaction Dynamics, and the University of Chicago reported on their findings from work conducted at the University of Chicago’s BioCARS 14-ID-B beamline at the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science user facility at DOE’s Argonne National Laboratory. Their results provide new structural and mechanistic insights to further illuminate this process.

The research focused on a light-sensing protein from the common oat plant, Avena sativa, called AsLOV2, a member of a superfamily of light-activated proteins that contain the light-oxygen-voltage (LOV) domain. These LOV domain-containing proteins detect blue light in the visible spectrum and have a conserved structure composed of five β sheets and four α helices. When blue light activates the chromophore, a covalent bond is formed between the light-sensing molecule and a cysteine amino acid on the protein. This is hypothesized to lead to protein dimerization and other conformational changes that transmit the light signal downstream.

The team used time-resolved X-ray liquidography (TRXL), a sensitive technique that can detect global conformational changes in solution on a millisecond to microsecond timescale, to analyze the light-activated transition of AsLOV2.

The structure of interest for the work was a piece of the full-length AsLOV2 protein that contained the LOV domain and two helices, A’α and Jα, that are known to be involved in the light-induced dimerization of the protein and downstream signaling. The team used a mutant–type of the protein (I427V) that has a faster recovery rate than the wild–type (WT) protein, facilitating some of the measurements. Kinetic evaluation of the TRXL data showed that light-induced transition of AsLOV2 includes ground (G), first intermediate (I1), second intermediate (I2), and final photoproduct (P) states with associated time constants (WT: 682 microseconds [μs] and 10.6 milliseconds [ms], and I427V: 130 μs and 3.4 ms).

Read more on APS website

SLS 2.0: How to start up a particle accelerator

SLS 2.0: How to start up a particle accelerator

The upgrade of the Swiss Light Source SLS, one of the large research facilities of the Paul Scherrer Institute PSI, is moving ahead: the electrons are back now in the completely new electron storage ring. A report from the SLS control room.

To switch on a large machine, just pressing a button is usually not enough. And the Swiss Light Source SLS is quite a remarkable machine: an accelerator-based large research facility that will soon resume producing high-intensity X-ray light for around 20 experiment stations at the Paul Scherrer Institute PSI. Thanks to the SLS 2.0 upgrade and a significantly slimmer electron beam, this light will be many times brighter and thus will enable better research than ever before. Now it is the beginning of 2025, and the facility is being awakened from its 15-month sleep. Step by carefully considered step.

“We tested the linear accelerator and the booster before Christmas and got them running again fairly quickly, which was encouraging,” says Jonas Kallestrup. He is an accelerator physicist who did his PhD at SLS, then worked at the Diamond Light Source in the United Kingdom for a few years and is now back at PSI since 2022. His main responsibility here is for the booster he mentioned: after the linear accelerator, this is the part of SLS that brings the electrons up to nearly the speed of light. From there they have to be brought into the electron storage ring. And from here, it gets exciting.

That’s because the electron storage ring, with a circumference of 288 metres, is brand new. As part of the SLS 2.0 upgrade project, it was replaced starting in October 2023. This means: a new vacuum tube within which the electrons can speed around almost undisturbed; a new, sophisticated arrangement of around 1,000 high-performance magnets along the ring, surrounding the vacuum tube to keep the electrons on their precise course; and new associated pipes and tubes, cooling systems, vacuum pumps, and a total of around 500 kilometres of cables to connect everything.

A landscape of number columns and diagrams

Kallestrup is part of the commissioning team, which these days is working with great concentration in the PSI control room in the building next to the SLS. Five to ten people typically sit here, some of whom were already part of the team when SLS was first commissioned in 2001. Eighteen large computer screens, each with a dozen application windows, are set up in a semicircle. Together they show a neatly arranged landscape of number columns and diagrams, enabling the team to keep an eye on the relevant parameters of SLS.

Masamitsu Aiba wrote his master’s thesis on particle accelerators 25 years ago. He later worked at CERN, and in 2009 he came to PSI. Now his specialty is injecting the electrons into the ring. “We’re about to see if all the new components fit together as precisely as we planned and calculated beforehand.” Aiba was himself involved in these detailed calculations – preparations for the renovation began several years ago.

On Tuesday, 14 January, the team succeeds in introducing the electrons into the first part of the storage ring. The particles do not get very far at first; which isn’t the first goal anyway. “It would be useless if we sent the electrons to do a full round once, but it was a bad round,” Aiba explains. The particles are so fast that, when SLS is operating, they fly through the entire ring a million times every second – even the smallest disturbance is noticeable. Actually storing the electrons in the ring only works if the first and therefore all subsequent rounds are as perfect as possible.

On his screens, Aiba can see exactly when the beam is not advancing well enough, and which magnet then needs to be adjusted and how. “Then we switch the machine off and confer with the people from the metrology group. They go into the accelerator tunnel and correct the magnets.” This part of the process is completely analogue, as screwdrivers are used to fine-tune individual permanent magnets until they are even better adjusted.

These new high-performance magnets are a crucial part of project SLS 2.0: the total number of magnets has been significantly increased; but where previously only electromagnets were installed, a large number of permanent magnets are now also in use. This makes the SLS a facility that is unique in the world and saves 60 percent energy compared to before. In addition, the permanent magnets reduce the noise that can affect the electron beam. All in all, the upgrade makes the electron beam 40 times better than before.

From a quarter of a lap to a million

On Wednesday, 15 January, the electrons are making it through the first quarter of the ring. One of the software windows on the second screen from the right displays a graphic with a row of 130 green dots, like pearls on a string. They show the measured values of the so-called beam position monitors, which register the position and intensity of the electron beam along the ring. The first 30 or so points have moved up, while all those behind them are still on the zero line – indicating how far the beam is getting so far. To make it farther, a few technical adjustments are now required.

Read more on PSI website

Image: Jonas Kallestrup, Masamitsu Aiba, and Felix Armborst (from left) in the PSI control room. They are part of the commissioning team that has now brought electrons back into the electron storage ring of the synchrotron as part of the SLS 2.0 upgrade project.

Credit: Paul Scherrer Institute PSI/Markus Fischer