Tag: COVID-19

Closing the door on colds and flu

Closing the door on colds and flu

First-of-its-kind structural data about protein family is key for drug discovery

New research by scientists at the University of Toronto and the Structural Genomics Consortium has deepened our understanding of how viruses like the flu, common cold, and COVID-19 get into cells in human airways.

Using the Canadian Light Source at the University of Saskatchewan, the researchers identified for the first time the crystal structures of a human protein (TMPRSS11D) that viruses use as a doorway into our body.

Understanding how viruses use our proteins to gain entry into our cells will help researchers develop better ways to stop infections in their tracks.

“This paper is really the stepping stone for building out more effective antiviral agents,” says lead author Bryan Fraser, a University of Toronto postdoctoral researcher at the Structural Genomics Consortium.

“We’re using the structure-based information that we’ve gained here to guide us in improving molecules that we hope will become drug candidates.”

Knowing the crystal structure of this “doorway” protein, says Fraser, is key to finding helpful drugs to stop coronavirus and influenza viruses, because it is very similar to other important proteins in the human body.

“Many of the important proteins for coagulation that are present in your blood look a lot like the TMPRSS proteins,” Fraser explains.

Successfully drugging subtle features on the TMPRSS proteins that are not present in coagulation proteins can be the difference between stopping infections and interfering with how wounds heal.

“The major challenge in our field is finding really effective compounds or drug candidates that show they’re selective for the target you’re interested in, and don’t block those other essential functions,” says Fraser.

While precise targeting is a challenge, the promise of these proteins as drug targets is immense.

Read more on CLS website

Newly created molecules block cytokine storm

Newly created molecules block cytokine storm

Cytokine storms are potentially life-threatening overreactions of the immune system provoked by viral infection and other “threats.” Two key players are cytokines interleukin-6 (IL-6) and interleukin-1 (IL-1). Currently available inhibitors of IL-6 and IL-1 relieve the cytokine storm associated with rheumatoid arthritis, but not with COVID-19. 

Now, scientists from the University of Washington have computationally designed protein inhibitors that may prevent the COVID-19-related cytokine storm. X-ray crystallography revealed a near-perfect match between the computational designs and their real-life counterparts, which blocked the cytokine storm in a human heart organoid. This suggests that computational design has the power to create entirely new proteins that function as viable therapeutics against the cytokine storm associated with COVID-19. 

Researchers used the resources of the Advanced Photon Source (APS), a U.S. Department of Energy (DOE) Office of Science user facility at DOE’s Argonne National Laboratory. 

Cytokine storm became a household term during the COVID-19 pandemic. Also known as cytokine release syndrome (CRS), this process happens when the immune system grossly overreacts to a threat and produces too many inflammatory immune cells. A cytokine storm can also be triggered by certain autoimmune diseases and CAR-T cell therapy.

The major players in a cytokine storm are cytokines IL-6 and IL-1. They bind to receptors on the surface of inflammatory immune cells, among others, sending signals to the cell’s DNA. These signals may activate the cell, amplify production of more inflammatory cells, or recruit cells to various locations. During a cytokine storm associated with COVID-19, too many inflammatory cells are activated and directed to the lungs and heart, where they can destroy tissue and cause fatal organ failure.

Binding is essential to the signal being sent; if there is no binding, there is no signal, and no cytokine storm. A few drugs on the market currently inhibit IL-6 and IL-1 binding, but they are better suited for long-term conditions like rheumatoid arthritis rather than short-term, acute events like COVID-19. To fill the void, a team of scientists led by 2024 Nobel Prize winner David Baker set out to design proteins from scratch that could effectively inhibit IL-6 and IL-1 binding. 

Both IL-6 and IL-1 rely on a third protein—GP130 in the case of IL-6, and an accessory protein in the case of IL-1—to send a signal when they bind with their receptors. The scientists used Rosetta, a proprietary protein design program, to create inhibitors that would occupy (a) binding sites on the IL-6 receptor, (b) the site on GP130 where IL-6 and its receptor would bind, and (c) the site on IL-1 where it would bind to both its receptor and the accessory protein.  

After generating their initial designs, the scientists tweaked them to improve the structure and amino acid sequence, then chose the top 100,000 candidates to test experimentally. First, they expressed the designs as real-life proteins in yeast cells. Then they optimized binding affinity by mutating each of the amino acids in the proteins. Finally, they used E. coli to express the optimized proteins. 

Read more on APS website

Image: Advances in computational design tools now enable functional proteins to be created from scratch.

Finding the chink in corona’s armour

Finding the chink in corona’s armour

The COVID-19 pandemic resulted in millions of deaths. Despite an unparalleled collaborative research effort that led to effective vaccines and therapies being produced in record-breaking time, a complete understanding of the structure and lifecycle of the coronavirus known as SARS-CoV-2 is still lacking. Scientists used the biolabs and the SPB/SFX instrument at the European XFEL to study the main protease, or Mpro, of the virus to understand how it protects itself from oxidative damage. The results add key knowledge to our understanding of the workings of SARS-CoV-2 and the field of viral biology.

Between January 2020 and March 2023, over six million people died as a result of the respiratory disease COVID-19, and several hundred million were infected. The disease is caused by SARS-CoV-2, a coronavirus. “Coronaviruses are a group of RNA viruses that cause illnesses and diseases in mammals and birds”, explains European XFEL scientist Richard Bean. “However, despite their significant relevance for global human health, there is still a lot to learn about the structure and function of coronaviruses in general and SARS-CoV-2 in particular.”

In response to the outbreak of the pandemic, scientists and scientific organizations around the globe poured efforts into studying the structure, dynamics, and function of SARS-CoV-2 in search of vaccines and therapies. Due to its central role in the replication cycle of the virus, the main protease – an enzyme that liberates newly made pieces of the virus from one another – soon emerged as a key antiviral drug target. The main protease, or Mpro, is particularly attractive for drug development because it plays a central role in viral replication, and also because it is quite different from all human proteins. This allows therapies to specifically target the virus while minimizing side effects that might harm patients. Previous drug discovery programmes targeting other viruses have succeeded using viral protease inhibitors, making a successful outcome in the case of SARS-CoV-2 more likely. “While the height of the COVID-19 pandemic may have passed, there is still a lot of value in studying the SARS-CoV-2 virus”, enhances Thomas Lane from the Center for Free-Electron Laser Science (CFEL) in Hamburg. “COVID continues to present a significant health threat worldwide. Given the persistence of this virus and the possible emergence of future pathogenic coronaviruses, it is imperative we develop a deeper understanding of Mpro and its role in viral function.”

In a recent experiment at the SPB/SFX instrument at the European XFEL, Lane and colleagues used the intense X-ray beam to study Mpro. Several previous structural studies focusing on Mpro have highlighted a number of peculiarities. “Firstly, the protein forms a 3D structure known as a dimer when it is found in high concentrations”, explains European XFEL scientist Robin Schubert, who was involved in the experiment. “This structural habit seems to directly influence its activity—but we don’t know precisely why this is important for the virus.”

Read more on XFEL website

Image: An understanding of the structure and lifecycle of the SARS-CoV-2 virus is essential to develop vaccines and therapies.

Credit: CFEL

Researchers visualise in 3D how SARS-CoV-2 replicates in cells

Researchers visualise in 3D how SARS-CoV-2 replicates in cells

The use of different microscopy and tomography techniques, including synchrotron light, unveils how lung cells are modified along the infection in cell culture models. The work is the result of the European consortium CoCID (Compact Cell Imaging Device) with the participation of CSIC groups and the ALBA Synchrotron.

The covid-19 pandemic has affected more than 770 million people and has caused the death of nearly seven million people around the world. Its huge impact on health and global economy has promoted research in the field since 2020, although it is still necessary to understand how this infection makes progress with the aim of finding specific solutions to this pathogen. Now, a team from the Spanish National Research Council (CSIC) and the ALBA Synchrotron publishes in the journal ACS Nano the results obtained after three-dimensional analysis of the interior of an infected cell.

Members of the National Centre of Biotechnology (CNB-CSIC) and the ALBA Synchrotron, the only synchrotron light source in Spain located in Cerdanyola del Vallès (Barcelona), have imaged in three dimensions the interior of human lung epithelium cells, the primary target of the virus, and the severe structural changes caused by SARS-CoV-2 infection.

Pablo Gastaminza, CNB-CSIC researcher and main author of the work, explains the alterations they found: “when comparing an uninfected cell with an infected one, we can see that the virus multiplication machinery forms vesicles and tubules as well as remarkable signs of stress on cellular organelles such as mitochondria and the endoplasmic reticulum.”

The study is part of the collaboration established within the European CoCID (Compact Cell Imaging Device) consortium. It combines the use of molecular biology, virology and three types of microscopy techniques. One of them is the so-called soft X-ray cryo-tomography (Cryo-SXT), a technology available only in four places all over the world, including the MISTRAL beamline at the ALBA Synchrotron. This technique allows “to generate three-dimensional maps of the ultrastructure of complete cells, reconstructing their total volume and providing extra information to other techniques like electron microscopy,” according to Eva Pereiro, head of the MISTRAL beamline at ALBA.

Read more on ALBA website

Image: Three-dimensional images of a fragment of a control cell (left) and a cell infected with SARS-CoV-2 (right). The cell nucleus is highlighted in purple, healthy mitochondria in green, and mitochondria modified by the infection in red, the vacuoles in light blue, the viral factory in yellow and the viral particles in blue. 

Credit: ALBA Synchrotron/CNB-CSIC

Funding for Diamond-II approved

Funding for Diamond-II approved

The Department for Science, Innovation and Technology together with Wellcome, one of the world’s largest biomedical charities, today (Wednesday 6th September) announced approval for the innovative update and expansion programme to the UK’s national synchrotron, Diamond Light Source, at a total project cost of £519.4M. The investment will see 86% come from the UK Government and 14% from Wellcome, the same proportion that has funded Diamond from its beginning.

The full approval of the upgrade, Diamond-II, is part of a major investment drive in cutting-edge facilities to keep UK researchers and innovators at the forefront of discovery and help address global challenges.  

Sir Adrian Smith, Chair of the Board of Diamond Light Source and President of the Royal Society comments:

We are delighted that the government and the Wellcome Trust have agreed this substantial investment in science infrastructure which will ensure the UK is at the forefront of world class science.  This investment in Diamond-II will strengthen the UK’s global scientific leadership and confirms the UK’s commitment to building on the success Diamond has achieved so far.

Secretary of State for Science, Innovation and Technology, the Rt Hon Michelle Donelan MP, said:

Our national synchrotron may fly under the radar as we go about our daily lives, but it has been crucial to some of the most defining discoveries in recent history – from kickstarting Covid drug development that allowed us to protect millions of Britons to advancing treatment for HIV.

Our investment will ensure one of the most pioneering scientific facilities in the world continues to advance discoveries that transform our health and prosperity, while creating jobs, growing the UK economy and ensuring our country remains a scientific powerhouse.

The overall transformational Diamond-II upgrade will take several years of planning and implementation. This will include a “dark period” of 18 months during which there will be no synchrotron light for the user community, followed by a period to fully launch the new facility with three new flagship beamlines and major upgrades to many other beamlines.

Read more on the Diamond website

Image: Touring Diamond’s experimental hall during celebrations to mark the funding announcement for Diamond-II.
L to R: Dr Richard Walker, Technical Director and Senior Responsible Owner for Diamond-II, Beth Thompson MBE Chief Strategy Officer at Wellcome, Dr Adrian Mancuso, Diamond’s Physical Science Director, Prof Sir Dave Stuart, Diamond’s Life Sciences Director,  Secretary of State for Science, Innovation and Technology, the Rt Hon Michelle Donelan MP, Sir Adrian Smith, Chair of the Board of Diamond, and Executive Chair of STFC Professor Mark Thomson.

Credit: Diamond Light Source

Treating COVID-19 by inhibiting viral replication

Treating COVID-19 by inhibiting viral replication

When SARS-CoV-2, the virus that causes COVID-19, enters a person’s cells, it hijacks those cells to make more viruses. First SARS-CoV-2 releases its RNA into the host cell. Then the host ribosomes translate the viral RNA into two giant protein chains (polyproteins). One protein in the giant chain, called MPro, cleaves the chain into smaller proteins, which help create more viruses and, therefore, more infection. Because of MPro’s role in initiating the viral replication process, the protein has become a target for antiviral drug developers. Recently, a team of scientists using high-brightness x-rays at the U.S. Department of Energy’s Advanced Photon Source (APS) has determined x-ray crystallographic structures of MPro cleaving the polyprotein at ten cleavage sites. Their findings, published in the journal Nature Communications, provide information about the mechanistic steps and molecular interactions that initiate viral replication, which can be used to inform antiviral therapeutic development for COVID-19, as well as other conditions for which MPro may be responsible.

Viruses can’t reproduce on their own; they need a human or animal cell to make other viruses and continue their infectious rampage. The SARS-CoV-2 virus, which causes COVID-19, employs its spike protein to enter a human cell. Once inside, the virus’s protective coating dissolves, and it dumps its genetic material—RNA—into the host cell. This RNA contains all the instructions the virus needs to replicate. What’s more, it comes in a handy form that is ready for a human cell to translate into proteins that will compose the next generation of viruses.

The SARS-CoV-2 RNA includes instructions for four proteins that make up the virus’s structure—its spike protein, protective coating, and the like—and sixteen proteins that replicate the virus. The replication process begins when the host’s ribosomes translate the replication genes into two gigantic protein chains called polyproteins.

Before replication can continue, however, these gigantic chains must be chopped up into their constituent proteins. Remarkably, the molecule that does the chopping is itself contained in the polyprotein and must hack its way out of the chain before attending to its neighbors.

Read more on the APS website

Image: Fig. 1. The amino acid residues preceding the SARS-CoV-2 polyprotein cleavage site between non-structural proteins nsp10 and nsp11 are shown in yellow. These residues are bound within the Mpro acceptor active site groove (grey semitransparent molecular surface).

Structural evidence that rodents facilitated the evolution of the SARS-CoV-2 Omicron variant

Structural evidence that rodents facilitated the evolution of the SARS-CoV-2 Omicron variant

The omicron variant of COVID-19 was identified in the fall of 2021. It stood out from all of the other variants because of the many mutations that simultaneously occurred in its spike protein1. So far, surveillance and bioinformatics have been the main scientific tools in tracking COVID-19 evolution. Eventually, however, understanding COVID-19 evolution comes down to understanding the functions of key viral mutations. This is where structural biology kicks in and plays a critical role in tracking COVID-19 evolution.

In a study recently published in the journal Proceedings of National Academy of Sciences USA, Dr. Fang Li and colleagues at the University of Minnesota determined the high-resolution crystal structure of the omicron strain’s spike protein and its mouse receptor (Fig. 1A)2, using macromolecular cystallography x-ray data measured at Beam Line 12-1 of SSRL. Through detailed analysis, the researchers identified three mutations (Q493R, Q498R, and Y505H) in the omicron spike protein that are specifically adapted to two residues (Asn31 and His353) in the mouse receptor (Fig. 1B, 1C). After searching all of the available receptor sequences in the database, the researchers found that only the receptor from mice contains Asn31 and His353, while the receptors from several other rodent species contain one but not both Asn31 and His353. Thus, the researchers hypothesized that rodents, particularly mice, played a role in the omicron evolution. In contrast, these three mutations in omicron are structurally incompatible with the corresponding two residues (Lys31 and Lys353) in the human receptor (Fig.1D, 1E)2, further suggesting that non-human animal reservoirs facilitated the omicron evolution.

Read more on the SSRL website

Image: Figure 1 (C) Structural details of the omicron RBD/mouse ACE2 interface showing Arg498 and His353 in omicron RBD are both structurally adapted to His353 in mouse ACE2.

Long COVID and pulmonary fibrosis better understood thanks to innovative techniques

Long COVID and pulmonary fibrosis better understood thanks to innovative techniques

An international team of researchers has revealed how scarring occurs in Long-COVID and pulmonary fibrosis using innovative blood biomarkers and X-ray technology. This study, published in The Lancet – eBioMedicine, contributes to the knowledge on the pathophysiology of severe COVID-19 and thus its treatment.

Long-COVID syndrome, or the origin of the long-term consequences of SARS-CoV-2 infection, is still not fully understood, more than two years after the onset of the pandemic. In particular, the long-term changes in lung tissue following severe COVID-19 disease pose significant limitations for many patients. Some of these patients continue to develop post-COVID pulmonary fibrosis, which is characterised by rapid scarring of the lung tissue.

Until now, the scientific community didn’t understand the underlying mechanisms of this scarring and of specific blood markers that can predict this process. Now, an international research team led by doctors and researchers at the Institute of Pathology at the RWTH Aachen University Hospital, the Hannover Medical School (MHH), HELIOS University Hospital in Wuppertal, and the University Medical Center Mainz, in collaboration with scientists at University College London (UCL) and the European Synchrotron (ESRF), has uncovered the mechanism that modifies the connective tissue of the lung in severe COVID-19. By combining the latest in imaging and molecular biology techniques this multidisciplinary team uncovered a mechanism by which the connective tissue of the lung is modified in severe COVID-19. They have demonstrated how COVID-19 changes the structure of the finest blood vessels in the lung and found molecular markers of this damage in the blood of patients that might ultimately help diagnose and treat the condition.

Read more on the ESRF website

Image: Two of the co-authors, Claire Walsh and Paul Tafforeau, during the scans and experiments at the ESRF, the European Synchrotron.

Unlocking the doors to effective COVID-19 treatments

Unlocking the doors to effective COVID-19 treatments

Developing therapeutics for COVID-19 should lessen the length and severity of the illness, keeping more people out of the hospital and improving patient outcomes.

A team of interdisciplinary researchers from the Institut National de la Recherche Scientifique (INRS) are hoping to identify effective COVID-19 therapeutics. With help from the Canadian Light Source (CLS) at the University of Saskatchewan, the team has been able to visualize the interaction between inhibitory molecules and viral proteins. This allows researchers to see if their drug designs work as intended.

“We have libraries of molecular fragments and drug candidates that we are testing,” said Michael Maddalena, a research intern in Steven LaPlante’s lab at INRS. “We are screening to see if they are active and actually stick to the virus’ proteins or to essential human receptors where we think there are opportunities for drugs.”

This research targets the proteins of the SARS-CoV-2 virus that are involved in its replication and survival. Their work also targets the essential human receptors that the virus depends on to enter human cells. Drugs that stick to human receptors are unlikely to be susceptible to viral mutants — ensuring that new therapeutics will be effective against new variants.

Read more on the CLS website

Image: The LaPlante research team

Natural substances show promise against coronavirus


Natural substances show promise against coronavirus

X-ray screening identifies compounds blocking a major corona enzyme

Three natural compounds present in foods like green tea, olive oil and red wine are promising candidates for the development of drugs against the coronavirus. In a comprehensive screening of a large library of natural substances at DESY’s X-ray source PETRA III the compounds bound to a central enzyme vital for the replication of the coronavirus. All three compounds are already used as active substances in existing drugs, as the team headed by Christian Betzel from the University of Hamburg and Alke Meents from DESY reports in the journal Communications Biology. However, if and when a corona drug can be developed on the basis of these compounds remains to be investigated.

“We tested 500 substances from the Karachi Library of Natural Compounds if they bind to the papain-like protease of the novel coronavirus, which is one of the main targets for an antiviral drug,” explains the study’s main author Vasundara Srinivasan from the University of Hamburg. “A compound that binds to the enzyme at the right place can stop it from working.”

The papain-like protease (PLpro) is a vital enzyme for virus replication: When a cell is hijacked by the coronavirus, it is forced to produce building blocks for new virus particles. These proteins are manufactured as a long string. PLpro then acts like a molecular pair of scissors, cutting the proteins from the string. If this process is blocked, the proteins cannot assemble new virus particles.

Read more on the DESY website

Image: The paper’s main author Vasundara Srinivasan at an X-ray set-up to test protein crystals in the lab.

Credit: University of Hamburg, Susanna Gevorgyan

New discoveries into how the body stores zinc

New discoveries into how the body stores zinc

Zinc deficiency is a global health problem affecting many people and results in a weak immune system in adults and especially in children. This is a challenge for health systems and is quite evident in the Mexican population, for example. Seeking explanations, researchers in Mexico teamed up with international synchrotron experts and gained new insights from studying Drosophila fruit flies, which are known to be a decent model system for human zinc metabolism.


Thanks to beamtime at BESSY II and at the SLS (PSI), they were able to show that the zinc stores in Drosophila flies depend on the tryptophan content of their diet.

“The first experiments were done on the KMC-3 spectroscopy beamline,” relates DFG Fellow Nils Schuth, who is currently researching in Mexico at the Center for Research and Advanced Studies of the National Polytechnic Institute (Cinvestav). “We took organs from a fruit fly and performed direct measurements of the tissue. We gained very revealing information from the data. That was the first step, which already brought us forward. In a second step, we then compared the biological results with various synthesised chemical complexes.”

The project started in 2019. Then came the pandemic and travel restrictions. The next measurements were therefore performed at the Paul Scherrer Institute (PSI) on the SLS, where the two research institutes were already cooperating. In the spring of 2021, new measurements performed at BESSY II confirmed their discoveries.

Read more on the HZB website

Image: Confocal images of the kidney-like Malpighian tubule from a Drosophila larva at two magnifications. More details in the main article.

Credit: © Erika Garay (Cinvestav)

Trigger of rare blood clots with AstraZeneca and other COVID vaccines found by scientists

Trigger of rare blood clots with AstraZeneca and other COVID vaccines found by scientists

understanding rare blood clots caused by some  COVID vaccines – important first to prevention

A collaborative team from the School of Medicine at the University of Cardiff, Wales and a range of US institutions used the UK’s national synchrotron, Diamond Light Source, to help reveal the details of how a protein in the blood is attracted to a key component of Adenovirus based vaccines.  

It is believed this protein kicks off a chain reaction, involving the immune system, that can culminate in extremely rare but dangerous blood clots. The Cardiff team were given emergency government funding to find the answers. In collaboration with scientists in the US and from AstraZeneca, they set out to collect data on the structure of the vaccines and perform computer simulations and related experiments to try and uncover why some of the vaccines based on Adenoviruses were causing blood clots in rare cases.  

Moderna and BioNTech are based on mRNA, whereas AstraZeneca and Johnson & Johnson are based on Adenoviruses. Blood clots have only been associated with vaccines that use Adenoviruses.

Read more on the Diamond website

Image: Crystallisation of ChAdOx1 fibre-knob protein results in 4 copies of the expected trimer per asymmetric unit and reveals side-chain locations. The crystal structure was solved with 12 copies of the monomer in the asymmetric unit, packing to form 3 trimeric biological assemblies. Density was sufficient to provide a complete structure in all copies.

Credit: Image reused from DOI: 10.1126/sciadv.abl8213 under the CC BY 2.0 license. 

#LightSourceSelfies – Light Source scientists are innovators

#LightSourceSelfies – Light Source scientists are innovators

Kathryn Janzen is an Associate Scientist and User Experience Coordinator at the Canadian Light Source. During her #LightSourceSelfie, Kathryn reflects on the light source community saying “The contacts between light sources are really important and everyone is very interested in sharing ideas. We’re also really interested in innovating and finding new ways to use the light source and finding new applications for old techniques.”

EBS X-rays show lung vessels altered by COVID-19

EBS X-rays show lung vessels altered by COVID-19

The damage caused by Covid-19 to the lungs’ smallest blood vessels has been intricately captured using high-energy X-rays emitted by a special type of particle accelerator.


Scientists from UCL and the European Synchrotron Research Facility (ESRF) used a new revolutionary imaging technology called Hierarchical Phase-Contrast Tomography (HiP-CT), to scan donated human organs, including lungs from a Covid-19 donor.


Using HiP-CT, the research team, which includes clinicians in Germany and France, have seen how severe Covid-19 infection ‘shunts’ blood between the two separate systems – the capillaries which oxygenate the blood and those which feed the lung tissue itself. Such cross-linking stops the patient’s blood from being properly oxygenated, which was previously hypothesised but not proven.


HiP-CT enables 3D mapping across a range of scales, allowing clinicians to view the whole organ as never before by imaging it as a whole and then zooming down to cellular level

Read more on the ESRF website

Image: Left: Scientists Claire Walsh, UCL and Paul Tafforeau, ESRF, during experiments at the ESRF, the European Synchrotron, France. (Credit S.Candé/ESRF)

Credit: S.Candé/ESRF

Insights into coronavirus proteins using SAXS

Insights into coronavirus proteins using SAXS

A collaboration led by researchers from the European Molecular Biology Laboratory (EMBL) used small angle X-ray scattering (SAXS) at the European XFEL and obtained interesting data on samples containing coronavirus spike proteins including proteins of the isolated receptor biding domain. The results can, for example, help investigate how antibodies bind to the virus. This gives researchers a new tool that may improve understanding of our bodies’ immune response to coronavirus and help to develop medical strategies to overcome COVID-19

SAXS is a powerful technique as it allows researchers to gain insights into protein shape and function at the micro- and nanoscales. The technique has proven to be extremely useful in investigating macromolecular structures such as proteins, especially because it removes the need to crystallize these samples. This means researchers can study the sample in its native form under physiological conditions under which biological reactions occur.

Read more on the European XFEL website

Image: Seen here, the instrument SPB/SFX, where the SAXS experiment was carried out. Using this instrument researchers can study the three-dimensional structures of biological objects. Examples are biological molecules including crystals of macromolecules and macromolecular complexes as well as viruses, organelles, and cells.

Credit: European XFEL / Jan Hosan

Research finds possible key to long term COVID-19 symptoms

Research finds possible key to long term COVID-19 symptoms

Key Points

  • Researchers from La Trobe University have identified a key mechanism that may link COVID-19 infection and lung damage
  • Lung damage is one of the possible long term effects of COVID-19
  • The macromolecular crystallography beamlines at the Australian Synchrotron continue to provide insights into the structural biology of COVID-19 

The Macromolecular and microfocus beamlines at the Australian Synchrotron continue to be an invaluable resource for studies in structural biology relating to COVID-19.

This week researchers from La Trobe University reported that they have identified a key mechanism in how SARS-CoV-2 damages lung tissue.

Some patients report long term-COVID symptoms affecting their breathing for months after recovering from an initial COVID-19 infection.

Read more on ANSTO website