For the past several months, teams of bioscientists have utilized Berkeley Lab’s world-class research facilities to contribute to the national response to COVID-19, resulting in a wide range of promising research. Four videos showcase researcher contributions from across the Biosciences Area, which aim to help address some of the many scientific challenges posed by the pandemic.
X-ray Experiments Zero in on COVID-19 Antibodies
Data gathered at Berkeley Lab’s Advanced Light Source (ALS) by an international team of researchers indicate that antibodies derived from SARS survivors could potently block entry of SARS-CoV-2 and other closely related coronaviruses into host cells. Such antibodies could be used as a preventative treatment or as a post-exposure therapy.
Ralston and Allaire Step Into New Roles
Corie Ralston and Marc Allaire, both staff scientists, have been promoted to new leadership positions. Ralston has assumed the position of Facility Director for the Biological Nanostructures Facility at the Molecular Foundry. Allaire has been appointed Head of the Molecular Biophysics and Integrated Bioimaging (MBIB) Division’s Berkeley Center for Structural Biology (BCSB). The BCSB manages six macromolecular crystallography beamlines at the Advanced Light Source (ALS).
Staff at ALS Mobilize to Support COVID-19-related Research
On March 31, a small team of staff at Berkeley Lab’s Advanced Light Source (ALS), which produces beams of X-rays and other types of light to support a wide variety of experiments for researchers around the world, launched several COVID-19-related experiments for other scientists who controlled the work remotely. X-rays allow researchers to map out the 3D structure of proteins relevant to diseases at the scale of molecules and atoms. Structural studies can lead to drugs that target and attack the virus while leaving other vital systems intact, for example, or that can otherwise improve the body’s defenses against the virus.
Cancer Drug Discovered with ALS Help Enters Phase 2 Trials
Seeking to develop a direct inhibitor of a mutant protein caused by errors in the KRAS gene, researchers at Amgen conducted X-ray crystallography of KRAS(G12C) proteins using the Berkeley Center for Structural Biology (BCSB) beamlines at the Advanced Light Source (ALS). The high-resolution structural maps generated from the data acquired revealed a small pocket on the molecule. Now, an investigational cancer drug that binds in this pocket will be evaluated in phase 2 clinical trials.
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