James Fraser

Biophysicist Faculty Scientist
Professor of Bioengineering and Therapeutic Sciences, UC San Francisco

Molecular Biophysics and Integrated Bioimaging

Structural Biology

jsfraser@lbl.gov
www.fraserlab.com

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Building Blocks for COVID-19 Antiviral Drugs Identified in Rapid Study

July 13, 2020

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.

NIH Awards $6.5 Million for Augmenting Structural Biology Research Experience

October 16, 2017

The National Institutes of Health (NIH) has awarded $6.5 million to Berkeley Lab to integrate existing synchrotron structural biology resources to better serve researchers. The grant will establish a center based at the Lab’s Advanced Light Source (ALS) called ALS-ENABLE that will guide users through the most appropriate routes for answering their specific biological questions.

Room Temperature XFEL Provides Clearest View Yet of Water Networks in Influenza M2 Proton Channel

August 23, 2017

Molecular Biophysics & Integrated Bioimaging (MBIB) Division scientists Aaron Brewster, Nicholas Sauter, and James Fraser were part of an international team led by William DeGrado at UCSF that used an X-ray free-electron laser (XFEL) source to visualize the arrangement of water molecules inside the influenza matrix 2 (M2) channel at room temperature. The M2 channel of influenza A is essential for the reproduction of the flu virus, making it a target for therapeutics, and it is also a model system for studying how protons are transported across a membrane bilayer. The XFEL method overcomes the limitations of previous crystallographic structures obtained using synchrotron radiation with cryocooling. While cryocooling helps to preserve crystals against rapid radiation damage, it imparts an artificially higher degree of order of the water molecules than structures obtained near room temperature. By using room temperature XFEL to study the M2 channel at various pH conditions, the researchers have gained a more accurate picture of the behavior of water molecules and their role in proton transport in these channels. The study was published in the Proceedings of the National Academy of Sciences.

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