Researchers search for clues to COVID-19 treatment

Two groups of researchers drew on SLAC tools to better understand how to target a key part of the virus that causes COVID-19

Vaccination, masks and physical distancing help limit the spread of COVID-19 – but, researchers say, the disease is still going to infect people, and doctors are still going to need better medicines to treat patients. This may be especially true for cancer patients and other at-risk people who may lack a sufficiently strong immune system to benefit from the vaccine. 

Now, two teams working in part at the Department of Energy’s SLAC National Accelerator Laboratory have found some clues that could, down the road, lead to new COVID drugs. 

The researchers, from John Tainer’s lab at MD Anderson Cancer Center and James Fraser’s group at the University of California, San Francisco, focused on a molecular structure that is common to all coronaviruses but has proven especially troublesome in the case of the virus that causes COVID-19. The structure contributes both to the virus’s ability to replicate and to immune system overreactions that have proven particularly deadly.

The trouble, Fraser said, is that scientists don’t know what kinds of molecules would bind to the structure, known as the Nsp3 macrodomain, let alone how to combine such molecules to interfere with its deadly work. 

To remedy that problem, Fraser’s group screened several thousand molecules at facilities including SLAC’s Stanford Synchrotron Radiation Lightsource (SSRL) to see where and how well the molecules bound to crystallized forms of Nsp3. The team combined those results with computer models to understand how the molecules might affect the structure of the macrodomain and whether they might help inhibit its function. 

Read more on the SLAC website

Virus recognition skills

A virus recognizes the starting point on the DNA to be packaged inside its protein shell

A bacteriophage – a virus that attacks bacteria – assembles into an infectious species using a powerful nanomachine to stuff its DNA into a protein shell. In several types of phage, this genome packaging motor is composed of several copies of large and small terminase subunits (TerL and TerS, respectively) that attach to a portal into the protein procapsid. 

Figure 1. Envelope of NV1 TerS from SAXS data, overlaid with modeled structure with open HTHs. Circle highlights one HTH motif.

The Cingolani group (Thomas Jefferson U) has now determined the structure of TerS from the Pseudomonas phage PaP3. Phage DNA to be packaged contains multiple copies of the genome, but just one copy is needed to fill a procapsid. Terminases attempt to package this one copy by various methods; in PaP3 a termination signal is provided by the interaction of a specific sequence in the DNA (the cos sequence) with TerS.

A crystal structure of PaP3 TerS reveals a nonameric ring of mixed alpha/beta composition, sitting atop a 9-stranded beta-barrel. Projecting out from the ring are spokes tipped with helix-turn-helix (HTH) DNA-binding domains. In the crystal, with no DNA present, the HTH domains are packed tightly against the inner parts of the nonamer (a “closed” form). Crystals of TerS from the related NV1 phage were also studied; their quality was not as good but the same conformation was found.  BioSAXS coupled to size-exclusion chromatography, at CHESS, was then used to examine the PaP3 TerS structure, and that of the related NV1 protein, in solution. Both turned out to be ~25% larger than predicted from the crystal structure. The molecular envelope determined from SAXS data for NV1 clearly showed protuberances on the outside of the nonameric ring that did not match the crystal structure. However, by rotating the HTH domain of each monomer about an obvious hinge region, an “open” model could be built that fit the SAXS envelope well (Figure 1). 

Read more on the CHESS website

Image: Figure 1. Envelope of NV1 TerS from SAXS data, overlaid with modeled structure with open HTHs. Circle highlights one HTH motif.

New insights into the photochemical activity of titanium dioxide

Not so many compounds are as important to industry and medicine today as titanium dioxide (TiO2). The electronic structure of transition metal oxides is an important factor determining the chemical and optical properties of materials. Specifically for metal-oxide structures, the crystal-field interaction determines the shape and occupancy of electronic orbitals. Consequently, the crystal-field splitting and resulting unoccupied state populations can be foreseen as modeling factors of the photochemical activity. The research on titanium dioxide inaugurated the presence of IFJ PAN scientists in research programs carried out at the SOLARIS synchrotron. The measurements, co-financed by the National Science Center, were carried out at the XAS beamline.

In many chemical reactions, TiO2 appears as a catalyst. As a pigment, it occurs in plastics, paints, and cosmetics, while in medical implants, it guarantees their high biocompatibility. A group of scientists from the Institute of Nuclear Physics of the Polish Academy of Sciences (IFJ PAN) in Krakow, led by Dr. Jakub Szlachetka, engaged in research on the oxidation processes of the outer layers of titanium samples and related changes in the electronic structure of this material. Scientists from the IFJ PAN conducted their latest measurements, co-financed by the National Science Center, at the XAS beamline. They analyzed how X-rays are absorbed by the surface layers of titanium samples previously produced at the Institute under carefully controlled conditions.

Read more on the SOLARIS website

Unravelling the molecular structure, self-assembly, and properties of a cephalopod protein variant

Cephalopods, such as the loliginid in Figure 1A, are known for their remarkable ability to rapidly change the color and appearance of their skin. These capabilities are enabled in part by unique structural proteins called reflectins, which play essential roles in optical behavior of cephalopod skin cells. Moreover, reflectins have demonstrated exciting potential as functional materials within the context of biophotonic and bioelectronic systems. Given reflectins’ demonstrated significance from both fundamental biology and applications perspectives, some research effort has been devoted to resolving their three-dimensional (3D) structures. However, the peculiar sequence composition of reflectins has made them extremely sensitive to subtle changes in environmental conditions and prone to aggregation, thus significantly complicating the study of their structure-function relationships and precluding their definitive molecular-level structural characterization. In this work, we have elucidated the structure of a reflectin variant at the molecular level, demonstrated a robust methodology for controlling its assembly and optical properties.


We began our studies by rationally selecting a prototypical reflectin variant (RfA1TV) by using a bioinformatics-guided approach (Figure 1B). Next, we not only produced the variant in high yield and purity but also optimized conditions for maintaining this protein in a monomeric state (Figure 1C). We then probed the protein with small angle X-ray scattering (SAXS) using the Austrian SAXS beamline at the Elettra Synchrotron Laboratory in Trieste, Italy. For this purpose, a well-dispersed solution of RfA1TV was prepared in a low-pH buffer and transferred into a glass capillary, which was positioned in the path of an incident X-ray beam. The X-rays scattered by the solution-borne RfA1TV molecules formed a 2-D pattern on a Pilatus3 1M detector (Figure 1D). Subsequently, radial averaging and image calibration of the two-dimensional data furnished corresponding one-dimensional curves, which were further processed, analyzed, and correlated with other experiments to obtain insight into the protein’s geometry (Figure 1E).

Read more on the Elettra website

Image: (A) A camera image of a Doryteuthis pealeii squid. (B) An illustration of the selection of the prototypical truncated reflectin variant (RfA1TV) from full-length Doryteuthis pealeii reflectin A1. (C) A digital camera image of a solution of primarily monomeric RfA1TV (Upper) and a corresponding cartoon of RfA1TV monomers (Lower Inset). (D) An illustration of the SAXS analysis of the reflectin variant, wherein incident X-rays are scattered by the solution-borne proteins to furnish a corresponding scattering pattern. (E)The 3D structure of RfA1TV (random coils – gray, helices – orange, β-strands – purple). 

Credit: This figure has been adapted from M. J. Umerani*, P. Pratakshya* et al.Proc. Natl. Acad. Sci. U.S.A 117, 32891-32901 (2020).

Microscopic origins of electrical conductivity in superheated solids revealed

Scientists used terahertz radiation for measurements of strongly excited material

In-depth understanding of the electrical conductivity of matter is the key to many cutting-edge research and applications, ranging from phase-change memory in microelectronics to magnetospheres rooted in planetary interiors due to the motion of the conductive fluid. Unique states of material created by ultrafast table-top lasers or free-electron lasers (FEL) allow us to gain insight into atomic levels. However, it also requires sub-picosecond resolution to capture the details on the timescale of atomic motion. Therefore, in conductivity measurements it prevents the use of contact diagnostics such as multimeter and four-point-probe. Although ultrafast optical or X-ray measurements can provide information on high frequency electrical conductivity, they require complex models to extrapolate the intrinsic direct current (DC) conductivity of material.

The terahertz radiation (1 THz= 1012 Hz (cycles per second)) offers a unique solution to tackle this dilemma. The THz electromagnetic wave behaves like DC electric-field to the sample because the oscillation of its electric field is slow compared to the electron momentum relaxation frequencies in solid and liquid materials (typically 1013Hz or larger), and the width of each THz cycle is short enough to resolve sub-picosecond dynamics. Nevertheless, to measure the conductivity of strongly excited materials in the irreversible regime still requires high brightness THz radiation in order to penetrate the dense electron cloud as well as high sensitivity to detect the THz temporal profile in a single shot.

An international research team, led by scientists from the SLAC National Accelerator Laboratory and DESY, have recently measured the electrical conductivity of strongly heated material using the THz FEL radiation at FLASH. In this study, gold nano-foil samples were heated by the FLASH extreme ultraviolet (XUV) FEL pulses to electron temperatures up to 16,000 °C. As the thermal energy transfers from the electrons to the ions, the sample transits from cold to superheated solid and eventually melts into warm dense liquid. The researchers have determined the DC electrical conductivity by measuring the transmitted THz electric field through the heated samples. The multi-cycle THz pulses from FLASH provide continuous measurements with temporal resolutions better than 500 femtoseconds.

Read more on the DESY website

Image: Artist’s impression: origins of the electrical conductivity in superheated solids measured with THZ radiation at FLASH at DESY

Credit: Z. Chen, SLAC

Promising candidates identified for COVID drugs

A team of researchers has identified several candidates for drugs against the coronavirus SARS-CoV-2 at DESY´s high-brilliance X-ray lightsource PETRA III. They bind to an important protein of the virus and could thus be the basis for a drug against Covid-19.

In a so-called X-ray screening, the researchers, under the leadership of DESY, tested almost 6000 known active substances that already exist for the treatment of other diseases in a short amount of time. After measuring about 7000 samples, the team was able to identify a total of 37 substances that bind to the main protease (Mpro) of the SARS-CoV-2 virus, as the scientists report online today in the journal Science. Seven of these substances inhibit the activity of the protein and thus slow down the multiplication of the virus. Two of them do this so promisingly that they are currently under further investigation in preclinical studies. This drug screening – probably the largest of its kind – also revealed a new binding site on the main protease of the virus to which drugs can couple.

Read more on the DESY website

Image: In the control hutch of the PETRA III beamline P11, DESY researcher Wiebke Ewert shows on a so-called electron density map where a drug candidate (green) binds to the main protease of the corona virus (blue).

Credit: DESY, Christian Schmid

The egg in the X-ray beam

Innovative time-resolved method reveals network formation by and dynamics of proteins.

A team of scientists has been using DESY’s X-ray source PETRA III to analyse the structural changes that take place in an egg when you cook it. The work reveals how the proteins in the white of a chicken egg unfold and cross-link with each other to form a solid structure when heated. Their innovative method can be of interest to the food industry as well as to the broad field of research surrounding protein analysis. The cooperation of two groups, headed by Frank Schreiber from the University of Tübingen and Christian Gutt from the University of Siegen, with scientists at DESY and European XFEL, reports the research in two articles in the journal Physical Review Letters.

Eggs are among the most versatile food ingredients. They can take the form of a gel or a foam, they can be comparatively solid and also serve as the basis for emulsions. At about 80 degrees Celsius, egg white becomes solid and opaque. This is because the proteins in the egg white form a network structure. Studying the exact molecular structure of egg white calls for energetic radiation, such as X-rays which is able to penetrate the opaque egg white and has a wavelength that is not longer than the structures being examined.

Read more on the DESY website

Image: When heated, the proteins in the originally transparent chicken egg white form a tightly meshed, opaque network.

Credit: DESY, Gesine Born

Riverine iron survives salty exit to sea

Iron organic complexes in Sweden’s boreal rivers significantly contribute to increased iron concentration in open marine waters, X-ray spectroscopy data shows. A Lund University study in Biogeosciences characterizes the role of salinity for iron-loading in estuarine zones, a factor which underpins intensifying seasonal algal blooms in the Baltic Sea.

The study ties in with a reported trend of increased riverine iron concentrations over the last decade in North America, northern Europe and in particular, Swedish and Finnish rivers. This, in conjunction with a predicted rise in extreme weather events in Scandinavia due to climate change, provides momentum for more bioavailable iron to enter marine environments such as the Baltic Sea.

“The consequences of increasing riverine iron for the receiving [marine] system depend first and foremost on the fate of iron in the estuarine salinity gradient. We had questions on what factors determine the movement and transport capacity of iron in these boreal rivers,” said Simon Herzog, postdoctoral researcher at Lund University.

The research group investigated the iron discharge in eight boreal rivers in Sweden which drain into the Baltic Sea, a brackish marine system. Water samples were taken upstream and at the river mouths, the latter just before estuarine mixing and stronger saline conditions occur. Spring and autumn specimens enabled the comparative analysis of flow conditions. To determine the type and amounts of iron species, measurements with X-ray absorbance spectroscopy (XAS) were taken at beamline I811 at Max-lab in Lund, Sweden and X-ray Absorption Near-Edge Structure (XANES) spectra at beamline ID26 at the European Synchrotron Radiation Facility (ESRF) in Grenoble, France.

Read more on the MAX IV website

Image: A view of the Ore River in northern Sweden

Credit: Simon Herzog

Battling bad bugs

Scientists fight antibiotic resistance by using synchrotron to study scab disease in potatoes.

In the ongoing war against antibiotic resistant bacteria, a change in battle tactics may prove effective for controlling a common disease of plants and potentially other toxins that affect humans and animals.

Although bacterial toxins cause serious, often deadly diseases, “bacteria aren’t trying to be nasty,” said Dr. Rod Merrill, Professor of Molecular and Cellular Biology at the University of Guelph. “They’re hungry and looking for food, and we’re often the food.” He added that 99 per cent of bacteria are helpful – like gut flora – so the battle is against the remaining one per cent.

The usual approach is to develop antibiotics “that kill the bacteria but not us, or the plant, or the animal,” stated Merrill. However, bacteria mutate quickly, as quickly as every 30 minutes, which leads to antibiotic resistance. “And unfortunately, the pipeline for new antibiotics is empty.”

The approach that Merrill and his research group are pursuing is an anti-virulence strategy – finding or designing small molecules that inhibit the tools bacteria use to colonize the host and create infection. “If we can put a lock on their weapons, they can’t get food and will move on so there’s not the same pressure to mutate. We’re going with this approach because we think it’s time to change up tactics.”

Read more on the CLS website

Image: Scabin crystals

Credit: CLS

New targets for antibodies in the fight against SARS-CoV-2

An international team of researchers examined the antibodies from a large cohort of COVID-19 patients. Due to the way antibodies are made, each person that is infected has the potential to produce many antibodies that target the virus in a slightly different way. Furthermore, different people produce a different set of antibodies, so that if we were to analyse the antibodies from many different patients, we would potentially be able to find many different ways to neutralise the virus.

The research article in the journal Cell is one of the most comprehensive studies of its kind so far. It is available online now and will be published in print on 15 April. These new results now show that there are many different opportunities to attack the virus using different antibodies over a much larger area than initially thought/mapped.

Professor Sir Dave Stuart, Life Sciences Director at Diamond and Joint head of Structural Biology at the University of Oxford, said:

SARS CoV-2 is the virus that causes COVID-19. Once infected with this virus, the human immune system begins to fight the virus by producing antibodies. The main target for these antibodies is the spike protein that protrudes from the virus’ spherical surface. The spike is the portion of the virus that interacts with receptors on human cells. This means that if it becomes obstructed by antibodies, then it is less likely that the virus can interact with human cells and cause infection.

By using Diamond Light Source, applying X-ray crystallography and cryo-EM, we were able to visualise and understand antibodies interact with and neutralize the virus. The study narrowed down the 377 antibodies that recognize the spike to focus mainly on 80 of them that bound to the receptor binding domain of the virus, which is where the virus spike docks with human cells.

Read more on the Diamond website

Image: Figure from the publication showing how the receptor binding domain resembles a human torso.

Credit: The authors (Cell DOI: 10.1016/j.cell.2021.02.032)

Game on: Science Edition

After AIs mastered Go and Super Mario, Brookhaven scientists have taught them how to “play” experiments at NSLS-II

Inspired by the mastery of artificial intelligence (AI) over games like Go and Super Mario, scientists at the National Synchrotron Light Source II (NSLS-II) trained an AI agent – an autonomous computational program that observes and acts – how to conduct research experiments at superhuman levels by using the same approach. The Brookhaven team published their findings in the journal Machine Learning: Science and Technology and implemented the AI agent as part of the research capabilities at NSLS-II.

As a U.S. Department of Energy (DOE) Office of Science User Facility located at DOE’s Brookhaven National Laboratory, NSLS-II enables scientific studies by more than 2000 researchers each year, offering access to the facility’s ultrabright x-rays. Scientists from all over the world come to the facility to advance their research in areas such as batteries, microelectronics, and drug development. However, time at NSLS-II’s experimental stations – called beamlines – is hard to get because nearly three times as many researchers would like to use them as any one station can handle in a day—despite the facility’s 24/7 operations.

“Since time at our facility is a precious resource, it is our responsibility to be good stewards of that; this means we need to find ways to use this resource more efficiently so that we can enable more science,” said Daniel Olds, beamline scientist at NSLS-II and corresponding author of the study. “One bottleneck is us, the humans who are measuring the samples. We come up with an initial strategy, but adjust it on the fly during the measurement to ensure everything is running smoothly. But we can’t watch the measurement all the time because we also need to eat, sleep and do more than just run the experiment.”

Read more on the Brookhaven website

Image: NSLS-II scientists, Daniel Olds (left) and Phillip Maffettone (right), are ready to let their AI agent level up the rate of discovery at NSLS-II’s PDF beamline.

Credit: Brookhaven National Lab

Building knowledge of changes in uranium chemistry

ANSTO’s considerable expertise in characterising uranium-containing compounds has contributed to a new systematic investigation of the origins of atomic structural distortions in a family of actinide compounds.

These compounds are known as rutile-related mixed metal ternary (three-part) uranium oxides. Rutile refers to mineral compounds composed primarily of titanium dioxide.

In research published in Inorganic Chemistry, a large team of researchers used both neutron and synchrotron radiation and theoretical calculations to establish systematically precise and accurate crystal structures and uranium oxidation states in the rutile-related mixed metal ternary uranium oxide systems.

Read more on the ANSTO website

Image:  Dr Zhaoming Zhang, Principal Research Scientist, Nuclear Fuel Cycle, ANSTO

Credit: ANSTO

Looking for photochemistry inside particles

At the Swiss Light Source (SLS), a new photochemical reaction cell was developed for the X-ray microscope at the PolLux beamline. This allowed the researchers to mimic sunlight mediated chemical reactions in airborne particles we normally inhale. Utilizing the new reaction cell, the X-ray microscope was used to image the interior of particles for the chemistry that produced a high concentration of persistent carbon centered radicals (CCR) and reactive oxygen species (ROS), which are harmful compounds when inhaled and can cause damage in the respiratory tract. Two main factors were 1) a very high particle viscosity that effectively locks the CCRs in a glass-like state and 2) oxygen deficiency, or anoxia, to prevent smaller ROS to be formed with a shorter lifetime that easily diffuse out of the particle before inhalation. When relative humidity in air is <60%, particles can become highly viscous or even glass-like, which drastically reduces the mobility of all molecules. Although sunlight induced radical formation is likely to be unhindered, high viscosity would instead inhibit molecular diffusion and block oxygen from accessing the particle interior. This leads to preservation of large amounts of radicals. Amazingly, this may apply to all organic light absorbing atmospheric compounds making radical abundance and persistence an unforeseen issue until now.

Particles composed of citric acid and iron were investigated as a model for iron containing organic particles. About 1 in 20 airborne particles contain iron in urban areas at a significant concentration as identified by previous studies. The oxidation state of iron was mapped across individual particles using X-ray spectromicroscopy to reveal where photochemical reactions, oxidation and molecular diffusion took place inside. Oxidation and formation of ROS took place rapidly, but surprisingly, only near the particle surfaces, i.e. an oxidized reaction front extending only hundreds of nanometers was directly observed. This was entirely due to the rapid depletion of oxygen in the particle due to slow molecular transport and fast reaction cycling. In addition to X-ray microscopy, the researchers used an electrodynamic balance (collaboration with ETHZ) and a coated wall flow tube reactor to study these radical forming particles and constrain the overall reactive cycle and the production and release of radicals to air.

Read more on the PSI website

Image: A chemical scheme and X-ray image showing particles oxidized only near their surface. Light in iron-organic particles start a cycle of oxidizing reactions (purple text) forming carbon centered radicals (yellow text) and reactive oxygen species (red text). We directly imaged oxidation happening only near the particle surfaces indicated by the brighter colour in micrometer and submicrometer viscous particles in the right image.

Credit: PSI

Expanding horizons with a new instrument

Work is in full swing to construct the new European XFEL instrument SXP. Manuel Izquierdo, who is the Group Leader for SXP since December 2020, gave insights into how the instrument will expand the European XFEL portfolio, when it is set to begin operations and what his vision is for the instrument at this stage.

How would you describe the SXP instrument?

SXP stands for “Soft X-ray Port”. This name was chosen in keeping with the core idea of the project, that is, to provide the users an FEL beamline where they can temporarily set up their own experiment stations. And, this is what makes the instrument unique: users can bring and operate their own experiment stations. This will allow many techniques and experiments to be implemented. The successful proposals would be those that cannot be performed at the two soft X-ray instruments SCS or SQS. So basically, the idea is that the SXP instrument will expand the portfolio of techniques available to users at European XFEL.

What kind of experiments will be performed at SXP? 

In principle it is up to the user community to suggest. So far, three communities have contributed to the project. One community aims to use European XFEL as a laboratory for astrophysics, atomic physics, and fundamental research investigating highly charged ions. A second community proposed studies on chemical bond activation in biological reactions and inorganic catalysts. The third and biggest community aims to perform time and angle-resolved photoelectron spectroscopy experiments in solids. This technique will allow understanding the atomic structure, chemical, electronic and magnetic properties of materials. The counter part for atoms, molecules and clusters can be done at the SQS instrument.

Read more on the European XFEL website

Image: Panorama view of the SASE3 beamline, which feeds SQS and SCS, and will now include SXP

Credit: Photograph by Dirk Nolle (Copyright: DESY)

Strong and resilient synthetic tendons produced from hydrogels

Human tissues exhibit a remarkable range of properties. A human heart consists mostly of muscle that cyclically expands and contracts over a lifetime. Skin is soft and pliable while also being resilient and tough. And our tendons are highly elastic and strong and capable of repeatedly stretching thousands of times per day. While limited success has been achieved in producing man-made materials that can mimic some of the properties of natural tissues (for instance polymers used as synthetic skin for wound repair) scientists have failed to create artificial materials that can match all the outstanding features of tendons and many other natural tissues. An international team of researchers has transformed a standard hydrogel into an artificial tendon with properties that meet and even surpass those of natural tendons. This new material was examined via electron microscopy and x-ray scattering to reveal the microscopic structures responsible for its outstanding features. The x-ray measurements were gathered at the U.S. Department of Energy’s (DOE’s) Advanced Photon Source (APS). The researchers have shown that their new hydrogel-based material can be modified to mimic a variety of human tissues and could also potentially be adapted to non-biological roles. Their results were published in the journal Nature.

Read more on the APS website

Image: Fig. 1. SEM images (left) showing the deformation of the mesh-like nanofibril network during stretching and corresponding in situ SAXS patterns (right). Scale bars, 1 μm (SEM images); 0.025 Å−1 (SAXS images)

Credit: From M. Hua et al., Strong tough hydrogels via the synergy of freeze-casting and salting out,” Nature 590, 594 (25 February 2021). © 2021 Springer Nature Limited

Researchers watch nanomaterials growing in real time

For the first time, a team of scientists including from DESY has succeeded in capturing in real time the first few milliseconds in the life of a gold coating as it forms on a polymer. The team used PETRA III to observe the earliest stages in the growth of a metal-polymer hybrid material as a film of gold was applied to a polymer carrier, in a process that can be used in industrial applications. The group’s research, which it presented now in the journal Nanoscale Horizons, not only offers important new insights into how innovative hybrid nanomaterials form, it also sets a new world record in the temporal resolution achieved using GISAXS, a surface-sensitive scattering technique.

Metal-polymer materials form the basis of modern flexible electronics, such as organic field effect transistors (OFET) or novel television screens (OLED). A detailed understanding of the manufacturing process is essential in order to manufacture such composites using smaller amounts of starting materials, to make them more energy-efficient and to be able to use them more flexibly.

Read more on the DESY website

Image: Experimental setup on beamline P03: The high-brilliance X-ray beam from PETRA III (magenta) is scattered by the surface structures while gold atoms are rapidly deposited on wafer-thin layers of plastic. The deflected X-ray light is recorded using a special high-speed camera designed at DESY. The sophisticated analysis of the real-time data obtained provides clues about the change in the sizes, distances and density profile of the resulting metal-polymer boundary layer

Credit: DESY/M. Schwartzkopf