A team of scientists, including many in the Molecular Biophysics and Integrated Bioimaging Division, uncovered new details about the reaction that powers photosynthesis. Understanding this reaction could lead to world-changing advances in technology, medicine, or energy––and also gives insight into how the enzyme photosystem II produces the oxygen we breathe. Their latest work was recently published in Nature Communications and two of the authors, Vittal Yachandra and Philipp Simon, spoke with Strategic Communications about that, shooting stuff with lasers, and why they chose this field of research.
New Refinement Technique Promises Greater Protein Structure Accuracy
X-ray free-electron lasers (XFELs) came into use in 2010 for protein crystallography, allowing scientists to study fully hydrated specimens at room temperature without radiation damage. Researchers have developed many new experimental and computational techniques to optimize the technology and draw the most accurate picture of proteins from crystals. Now scientists in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division have developed a new program, diffBragg, which can process every pixel collected from an XFEL for a protein structure independently. In a recent IUCrJ paper, the team led by MBIB Senior Scientist Nicholas Sauter proposed a new processing framework for more accurate determination of protein structures.
Building Blocks for COVID-19 Antiviral Drugs Identified in Rapid Study
Members of the UC San Francisco Quantitative Bioscience Institute Coronavirus Research Group (QCRG), in collaboration with Berkeley Lab and SLAC National Accelerator Laboratory (SLAC), have identified key chemical building blocks for an eventual antiviral drug against SARS-CoV-2, the virus that causes COVID-19. The newly identified compounds bind to an enzyme produced by the virus, called the “macro domain,” which is known to be crucial for the virus’s ability to replicate in human cells. The authors are writing up a formal manuscript describing the results for submission to a peer-reviewed academic journal, but also published their data directly online on July 1 to accelerate global efforts to fight the coronavirus pandemic.
James Holton Named ACA David J. Rognlie Award Winner
James Holton, a faculty scientist in the Molecular Biophysics and Bioimaging (MBIB) Division and full adjunct professor of biochemistry and biophysics at the University of California, San Francisco (UCSF), is the 2020 recipient of the American Crystallographic Association’s David J. Rognlie Award.
Toward a Blueprint for Anti-influenza Drugs
An international team led by researchers at UCSF used protein crystallography at the Advanced Light Source (ALS) beamline 8.3.1 to obtain structures of several influenza antiviral drug molecules bound to their proton-channel targets in both open and closed conformations. These complexes provide the first high-resolution views of how the drugs interact with and disrupt the water-molecule networks lining the M2 transmembrane channel. The structures provide an atomic-level blueprint from which to design more effective anti-influenza drugs that can overcome growing drug resistance. ALS beamline 8.3.1 is operated by James Holton, MBIB beamline scientist and associate adjunct professor at UCSF.
Read more in the ALS Science Highlight.
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