MBIB News

Six Biosciences employees have been selected by the Women Scientists and Engineers Council (WSEC) and the Diversity, Equity, and Inclusion (DEI) Office for recognition as part of the third Women @ The Lab awards. The program spotlights women at the Lab who demonstrate dedication, talent, STEM contributions, and commitment to the Lab’s mission.

CASP is the Critical Assessment of Protein Structure Predictions, a biannual “competition” to determine which prediction algorithm generates the most accurate model. There are several categories in which models will be assessed, including accuracy, topology, and biological relevance. The SIBYLS beamline is participating to provide small-angle X-ray scattering (SAXS) data for––and judging for the first time––the “data-assisted” category. This CASP competition should lead to improvement in predicting protein-protein interfaces and complex structures.

The Advanced Light Source hit a structural biology milestone in May 2018 with the help of their eight structural biology beamlines. Users of these beamlines have now collectively deposited over 7000 proteins into the Protein Data Bank (PDB), a worldwide, open-access repository of protein structures. The 7000th ALS protein structure (PBD accession number 6C7C) is an enzyme from Mycobacterium ulcerans (strain Agy99), solved with data from Beamline 5.0.2 in the Berkeley Center for Structural Biology. The enzyme is of interest to the researchers from the Seattle Structural Genomics Center for Infectious Disease (SSGID), whose mission is to obtain crystal structures of potential drug targets on the priority pathogen list of the National Institute of Allergy and Infectious Diseases (NIAID). Beamline 5.0.2, the first protein crystallography beamline at the ALS, came online in 1997. Read more in the ALS Feature.

Jill Fuss and Steve Yannone, both research scientists in Molecular Biophysics and Integrated Bioimaging (MBIB), are among the 13 scientists and engineers who comprise the fourth cohort of Cyclotron Road fellows. The pair co-founded CinderBio, a spin-out company that uses extremophile microbes to produce industrial enzymes that can withstand very high temperatures and acidic environments.

Researchers at Berkeley Lab and UC Berkeley have combined cutting-edge cryo-electron microscopy (cryo-EM) with computational molecular modeling to produce a near atomic-resolution model of the interaction between microtubules—crucial components of eukaryotic cell ultrastructure—and microtubule-associated proteins called tau. The model provides insight into how tau stabilizes microtubules, and what makes it dissociate to form tau aggregates, or “tangles,” in some neurological diseases—including Alzheimer’s disease—generally referred to as tauopathies.