A team of UC Berkeley and Berkeley Lab researchers used X-ray crystallography performed at the Advanced Light Source (ALS) to determine the atomic structure of ORF8, a protein secreted by the SARS-CoV-2 virus that is thought to help the pathogen evade and dampen response from human immune cells.
Experimental Drug Targets HIV in a Novel Way
Using Berkeley Center for Structural Biology (BCSB) beamline 5.0.1, researchers from Gilead Sciences investigated a promising small-molecule drug, GS‑6207, that they developed to inhibit replication of the human immunodeficiency virus (HIV).
Videos Showcase Biosciences’ Response to COVID-19
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.
Rotavirus VP3 Is a Multifunctional Capping Machine
Combining cryo-electron microscopy, biochemical assays, and protein crystallography at Advanced Light Source (ALS) Beamline 5.0.2 (part of the Berkeley Center for Structural Biology), researchers from the Baylor College of Medicine discovered that rotavirus VP3 incorporates in one place all the enzymatic activities required to effectively cap rotavirus mRNA, making it unique among viral-capping enzymes.
Finding the Missing Step of an Important Molecular Process
Lysine is an important amino acid that must be supplied in our diets, as our bodies can’t produce lysine on their own. Most cereal grains have low levels of lysine, and scientists have worked to breed crops with higher lysine levels.
However, the biochemical processes that break down lysine in plants weren’t fully understood. New Joint BioEnergy Institute (JBEI) research, published in Nature Communications, reveals this last missing step of lysine catabolism.
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