ARIEs as key resources for the five Horizon Europe Missions

Moon-shot missions, such as those of Horizon Europe, require exceptional solutions, and the world-leading Analytical Research Infrastructures of Europe (ARIEs) are one of the key places those solutions can be sought. The ARIE Joint Position Paper highlighting how the common, complementary approach will help address the societal challenges of the Horizon Europe Missions framework programme was presented today.

“The Analytical Research Infrastructures of Europe (ARIEs) provide unique windows into the workings of the world around us”, says Caterina Biscari, Chair of LEAPS and Director of the ALBA Synchrotron in Spain. “The cross-border cooperation within Europe allows for harnessing the power of its analytical research infrastructures collectively, to fuel the cutting-edge R&D required by the five Horizon Europe Missions. Nowhere else in the world is this readily possible.”

The ARIEs are centres of scientific and technological excellence, delivering services, data and know-how to a growing and diverse user community of more than 40,000 researchers in academia and industry, across a range of domains: the physical sciences, energy, engineering, the environment and the earth sciences, as well as medicine, health, food and cultural heritage. They include powerful photon sources, such as synchrotrons, laser systems and free-electron lasers; sources of neutrons, ions and other particle beams; and facilities dedicated to advanced electron-microscopy and high magnetic fields.

Read more on the MAX IV website

X-ray beams help seeing inside future nanoscale electronics

The technological advancement of fourth-generation synchrotrons, pioneered by MAX IV Laboratory, opens research opportunities that were impossible just a few years ago. In a newly published research paper, we get proof of the revolutionary impact that MAX IV’s photons can have for the advancement of nanoelectronics, both in research and for industrial manufacturers.

Thanks to the innovative concept of the multi-band achromats, MAX IV Laboratory has paved the way for fourth-generation synchrotrons and as of now, it is the most brilliant source of X-ray for research. The high coherence and brilliance delivered at MAX IV are giving scientists the tools for performing research previously unachievable in the X-ray spectrum. This potential is highlighted in a new publication centred on investigating innovative non-destructive characterization of embedded nanostructures.

Read more on the MAX IV website

Image: Depiction of the process of nanofocused X-ray beams scattering from a single nanowire transistor. Positively charged particles (+) and negatively charged particles (-) represent charge carriers in a p–n junction (where p–n junction is an interface between p-type and n-type semiconductor materials). Outgoing beams, depicted as white rays, represent scattering from different segments of the device (InAs and GaSb). The bending with arrows represents the strain revealed in the experiment.

Credit: Illustration by Dmitry Dzhigaev, Lund University.

Atomic vibrations play key role in material phase change

A research group working with MAX IV’s FemtoMAX beamline has succeeded to slow the phase change from the solid to liquid state in the semiconductor, indium antimonide (InSb), by reducing the inherent vibrations between atoms. An important precursory step in the process was non-thermal melting of the sample, which broke its atomic bonds. This revealed that unbound atoms move with the velocity they had at the instant the bonds were broken. Further it showed that initial velocity is governed by atomic vibrations, which in turn are temperature dependent. The findings are steps toward functional manipulation of material structure during phase transitions.

Imagine a world where we control the structure of materials by subjecting them to short-pulse laser radiation. This is the implication of research that allows us to alter the timing when phase change occurs.

Melting a material with or without heat produces a similar result, at a similar speed. What is going on at the atomic level is quite different, however. Thermal heating excites electrons to a higher energy state. Electron-phonon coupling then equilibrates the electron and lattice temperature which makes the lattice vibrate so violently that atomic bonds break. Non-thermal heating also excites electrons but breaks the bonds instantly—within femtoseconds—and releases atoms from their original structural configuration. Scientists seek to distinguish what happens after bonds sever due to these excited electrons.

Read more on the MAX IV website

Image : FemtoMAX beamline at MAX IV

An innovative mirror unit for soft X-ray beamlines at MAX IV

A new five-axis parallel kinematic mirror unit has been developed for MAX IV soft X-ray beamlines. Its development and technical characteristics are now described in a peer-reviewed article.

A new five-axis parallel kinematic mirror unit has been developed for MAX IV soft X-ray beamlines. Its development and technical characteristics are now described in a peer-reviewed article.

In an article published in March 2020 in the Journal of Synchrotron Radiation, a team from Uppsala University, MAX IV Laboratory, FMB Feinwerk und Messtechnik GmbH, and University of Tartu presents a five-axis parallel kinematic mirror unit specially developed for MAX IV soft X-ray beamlines. This new mirror unit has been created to address the unique stability requirements of 4th-generation synchrotrons such as MAX IV.

MAX IV has pioneered the development of the 4th-generation synchrotrons thanks to the implementation of the multi-bend achromat technology, a system based on the use of several sequential bending magnets in place of a single large magnet. Thanks to the introduction of this technology, the emittance has decreased by one order of magnitude, resulting in increased brightness. The multi-bend achromat system has also brought new challenges for the construction of beamlines. Decreased emittance of the storage ring has allowed for a smaller beam size, which, in turn, means higher requirements for electron beam stability, as well as for mechanical stability of the beamline components.

>Read more on the MAX IV website

Image: Veritas is one of the beamlines at MAX IV used for testing the prototype of the new five-axis parallel kinematic mirror.

A revolutionary setup for atomic layer deposition at SPECIES

In a joint project across three universities and MAX IV laboratory, researchers have developed a revolutionary experimental setup for atomic layer deposition.

The new instrument was designed specifically for MAX IV and will allow for observations previously impossible.
SPECIES, one of the soft X-ray beamlines in MAX IV 1.5 GeV storage ring, has added to its portfolio a new cutting-edge instrument. The new experimental setup has been specially developed to use Ambient Pressure X-ray Photoelectron Spectroscopy (APXPS) for the study of atomic layer deposition (ALD), a process where thin films of material are grown depositing one layer at a time.

This experimental setup is composed of a custom cell where the ALD process is performed and observed using APXPS. The instrument is the result of an extensive collaboration between the University of Helsinki, world-leading in ALD studies, University of Oulu, Lund University, and MAX IV Laboratory, and funded by the University of Helsinki through the FiMAX consortium.
In February, the team from the University of Helsinki led by professor Mikko Ritala, and from the University of Oulu came to MAX IV for the final experiments and refinement activities on the experimental setup. We talked with the scientists to understand how the cell they have developed allows for unprecedented observations.

>Read more on the MAX IV website

Image credit: Matti Putkonen.

Beyond graphene: monolayer arsenene observed for the first time

An article recently published in 2D Materials shows the first experimental evidence of the successful formation of arsenene, an analogue of graphene with noteworthy semiconducting properties.

This material shows a great potential for the development of new nanoelectronics. Crucial sample preparation and electron spectroscopy experiments were performed at the Bloch beamline at MAX IV.

The discovery of graphene, the single-layer carbon honeycomb material worth the Nobel Prize in Physics in 2010, surely has had a revolutionary impact on research. It triggered a whole new field of study within two-dimensional (2D) materials. However, its application in developing new 2D electronics has been hindered by its lack on an intrinsic band gap. Researchers therefore started to turn their attention to other elements in the periodic table and set their eyes on group V, to which arsenic belongs.
“The aim of the study was to show that arsenene can be formed. Our article is the first to report this”, says Roger Uhrberg, professor at Linköping University and spokesperson for the Bloch beamline at MAX IV. Arsenene, a single-layer buckled honeycomb structure of arsenic, had been previously predicted by various theoretical studies, but this is the first experimental observation that verifies its existence.

>Read more on the MAX IV website

Image: A view of the Bloch beamline at MAX IV. The Bloch beamline consists of two branchlines, and is dedicated to high resolution photoelectron spectroscopy, encompassing angle-resolved (ARPES), spin resolved (spin-ARPES) and core-level spectroscopy.

The role of synthesis gas in tomorrow’s sustainable fuels

In a new publication in Nature Communications, a team from the Dutch company Syngaschem BV and the Dutch Institute for Fundamental Energy Research elucidates for the first time some aspects of the Fischer-Tropsch reaction, used for converting synthesis gas into synthetic fuels.

Analysis performed at HIPPIE beamline at MAX IV were instrumental to achieve these results. The adoption of sustainable and renewable energy sources to permanently move beyond the dependence from fossil fuels constitutes one of the great challenges of our time. One that is made more urgent by the effects of climate change we witness on a daily basis. Electrification, such as we see in the development of electric vehicles, seems a promising strategy, but it cannot be the solution for all applications. In many cases liquid fuels are still considered the best and most efficient option. Is there a way to produce liquid fuels in an efficient and sustainable manner, one that does not rely on fossil sources?

>Read more on the MAX IV website

Discovering a whole new family of copper-binding proteins

While studying a class of copper-containing enzymes, a team of researchers discovered and characterised a new family of fungal proteins.

Their study has now been published on Nature Chemical Biology, including analysis performed at BioMAX. The article is published together with a parallel study that sheds light on one of the potential biological roles of the proteins in this new family.

In contrast with a certain romanticised idea of research, scientific discoveries seldom come with a shouted “eureka!” as to mark the end of a linear intellectual endeavour. Much more frequently, new scientific findings emerge from observations where a scientist’s first reaction might sound like “that’s odd…”. Perhaps that was how the authors of this study reacted when they realised what they were looking at wasn’t what they were looking for.

In an article published this week on Nature Chemical Biology, a team of scientists from INRA, University of Copenhagen, Marseille Université, and University of York characterised a new family of proteins, named X325, found in various fungal lineages. The article is published together with a parallel study in which one protein of this new family, Bim1, is described as involved in fungal meningitis.

The authors were initially searching for new lytic polysaccharide monooxygenases (LPMOs), copper-dependent enzymes specialised in the degradation of polysaccharides and widely used in the production of biofuels. The proteins of this new family seemed promising candidates since they share many structural features and a probable common ancestor with LPMOs. However, the researchers proved that the members of this LPMO-like protein family are not involved in polysaccharides degradation, but they more likely play a role in the regulation of copper ion content in the organisms where they are expressed.

>Read more on the MAX IV website

Image: Copper binding site of two different proteins. Left: LaX325 protein belonging to the newly identified LPMO-like protein family X325. Right: cellulose cleaving LPMO enzyme TaAA9.
Image developed by Tobias Tandrup, University of Copenhagen.

First delivery of single-bunch electron beam to the 1.5 GeV ring

The 22 October at lunchtime, the first single-bunch electron beam was delivered to the 1.5 GeV storage ring at MAX IV and put to use at the FinEstBeAMS beamline.

These are still preliminary trials and the response from FinEstBeAMS will determine the path forward.

Normally the electrons in the storage rings come in so-called multi-bunch formation. You could think of this as several locomotives with many wagons travelling around the ring. In single-bunch mode, there is only one locomotive “on the track”. The abstract of Christian Strålman’s PhD thesis On the Challenges for Time-of-Flight Electron Spectroscopy at Storage Rings gives a good overview of the topic in Swedish.

The single-bunch mode will give the scientists access to a wider portfolio of measurement techniques in several research areas such as atmospheric chemistry, environmental science (in particular renewable energy sources), molecular reaction dynamics, cluster chemistry and physics, materials science, chemistry–chemical reactions at surfaces or in solution and photocatalysis.

>Read more on the MAX IV website

Image (extract):A screenshot of a scope measurement of the current in the ring, where you can clearly see the strong single-bunch signal. See full image here.

Discoveries map out CRISPR-Cas defence systems in bacteria

For the first time, researchers at the University of Copenhagen have mapped how bacterial cells trigger their defence against outside attacks. This could affect how diseases are fought in the future.

With the aid of highly advanced microscopes and synchrotron sources, researchers from the University of Copenhagen have gained critical insight into how bacteria function as defence mechanisms against attacks from other bacteria and viruses. The study, which has just been published in the renowned journal, Nature Communications, also describes how the defence systems can be activated on cue. This discovery can turn out to be an important cornerstone in fighting diseases in the future.

The researchers have shown how a cell attacked by a virus activates a molecule called COA (Cyclic Oligoadenylate), which in turn activates a so-called protein complex called CSX1 to eradicate the attacker.

>Read more on the MAX IV website

Image: Model of the CSX1 protein complex.

New research possibilities at NanoMAX

X-rays can penetrate materials and are therefore useful for studying chemical processes as they occur inside reactors, cells, and batteries. A common ingredient in such chemical systems is metal nanoparticles, which are often used as catalysts for important reactions. As the NanoMAX beamline provides a very small X-ray focal spot, single nanoparticles can in principle be studied as they perform their catalytic functions.

In this paper, we show that gold nanoparticles sitting inside an electrochemical cell can be imaged at NanoMAX. These preliminary results come from nanoparticles around 60 nm (60 millionths of a millimetre) in size, and we show that even smaller particles could be studied. If successful, future experiments will allow “filming” nanoparticles as they catalyze reactions in real-time, and give new understanding of how catalysis works. That could in turn help design new materials for energy conversion, chemical production, and water purification.

>Read more on the MAX IV Laboratory
Image (extract, full image here): Coherent Bragg imaging of 60 nm Au nanoparticles under electrochemical control at the NanoMAX beamline

Collaboration develops sensitive data protocol

MAX IV pairs up with Sprint Bioscience, a listed drug development company, in a new project to improve how companies can benefit from new, faster X-ray fragment screening experiments, while still protecting their valuable information during analysis at FragMAX.

Recently, the project was granted with 500 000 SEK from Sweden’s innovation agency Vinnova.
More or less, all pharmaceutical drugs are molecules binding to proteins in your body. When doing this, they either initiate or inhibit the process in which the target protein is involved. Proteins are in charge of everything from cells dividing at the right moment to the metabolism of the food you eat or signaling in the brain.

>Read more on the MAX IV website

Image: Sample holders
Credit: Ben Libberton

17 meter long detector chamber delivered to CoSAXS

The experimental techniques used at the CoSAXS beamline will use a huge vacuum vessel with possibilities to accommodate two in-vacuum detectors in the SAXS/WAXS geometry.

A major milestone was reached for the CoSAXS project when this vessel was recently delivered, installed and tested.
The main method that will be used at the CoSAXS beamline is called Small Angle X-ray Scattering (SAXS). By detecting the scattered rays coming from the sample at shallow angles, less than 4° typically, it is possible to learn about the size, shape, and orientation of the small building blocks that make up different samples and how this structure gives these materials their properties. The materials to be studied can come from various sources and in diverse states, for example, plastics from packaging, food and how it is processed or proteins in solution which can be used as drugs.
The “co” in CoSAXS stands for coherence, a quality of the synchrotron light optimized at the MAX IV machine, that loosely could be translated as laser-likeness. In the specific case of X-ray Photon Correlation Spectroscopy (XPCS), it lets the researchers not only measure the structure of the building blocks in the sample but also their dynamics – how they change in time.

>Read more on the MAY IV Laboratory website

New beamline for electron bunch diagnostics

A new diagnostic beamline connected directly to the MAX IV linear accelerator is under construction.

It will enable time-resolved characterization of primarily the ultrashort electron bunches for the FemtoMAX beamline but will also be useful for other time-resolved experiments. The design of the highly specialized beamline components is to a large part done in-house.
Head up and tail down
The linear accelerator accelerates electrons up to high energies. Short bunches containing 109 electrons are delivered from the linear accelerator to make X-ray pulses for the FemtoMAX beamline. The duration of the bunches is in the femtosecond (10-15 s) regime to enable high temporal-resolution measurements at the beamline. The short duration makes the bunches very challenging to characterize with time resolution as conventional detection devices are too slow.
In the new setup, two so-called transverse deflecting cavities (TDC) will make the acquisition of time-resolved data possible. They will in principle add an electromagnetic field that deflects the head of the electron bunch upwards and the tail down so that the first electrons hitting the beam profile analyzer will end up at the top of the screen and the last ones will end up at the bottom. The resulting streak gives a time-resolved measurement of the shape of the bunch but the method will also be used to characterize for example how emittance and energy vary as a function of time.
– Today we rely on calculations and relative measurements for the bunch length delivered to FemtoMAX says project leader Erik Mansten, the TDC is a way for us to verify what we deliver. It also helps us preparing the linac for a possible free electron laser in the future.

>Read more on the MAX IV website

Image: These copper disks are going to become transverse deflecting cavities for the new diagnostic beamline.

Why having your head in the clouds could be a really good thing

The ATMOS research group in the NANOMO unit, led by Nønne Prisle, Associate Professor at the University of Oulu, are trying to find out what kind of chemistry is happening in cloud droplets and tiny nanometer-sized aerosol particles in the atmosphere. This knowledge could eventually, hopefully, give us more accurate theoretical models to understand the ongoing climate change.
– The only thing that can halter climate change is to stop emitting CO2. Nønne Prisle is very, very clear on that. Even so, she says, if we want to take any other step to try to counter climate change, we really need to know what’s going on in the clouds since these processes could be quite critical.
The ATMOS team are using the beamline HIPPIE at MAX IV being so-called commissioning experts, which means that the experiment is done both to provide useful data but also to verify the capacity and capability of the beamline experimental station.

>Read more on the MAX IV Laboratory website

Image: From left to right: Robert Seidel, Helmholtz Zentrum Berlin; Nønne Prisle, Kamal Raj and Jack Lin, University of Oulu at the HIPPIE beamline.

Capturing protein motion at FemtoMAX

Your body contains a large variety of different proteins. They are big, complex molecules with diverse functions, from transporting oxygen in your blood to making your muscles contract.

Many proteins change their shape and move as they perform their task. A research team from the University of Gothenburg recently visited the beamline FemtoMAX to develop a method for studying moving proteins. They use electric fields to stimulate motion of the proteins in a sample while imaging them with the X-ray beam.
To study how proteins move, we need something to nudge them and then image them after they have changed position. Certain proteins are activated by light and in that case, the researchers can hit them with a laser pulse to provoke the motion. However, that is far from always the case. In the method being developed by the Gothenburg team, the proteins are instead subjected to an electric field that make them move.
The field is synchronized to the short, femtosecond scale (10-15 s) X-ray pulses delivered at beamline FemtoMAX. Each X-ray pulse hitting the sample is like taking a photograph using extremely short shutter speed, just like trying to get sharp images of players on a football field. The X-ray pulses at FemtoMAX are short enough to let the researchers capture the instantaneous position of the protein. By varying the time between the electric field and the X-ray pulse they can see different stages of the movement and even put the frames together as a movie of the protein motion.

>Read more on the MAX IV Laboratory website