A team led by Mary Estes of the Baylor College of Medicine used rotavirus as a model to study some of the proteins involved in making the cytoplasmic compartments in which many DNA and RNA virus pathogens replicate. Banumathi Sankaran, a research scientist in the Berkeley Center for Structural Biology (BSCB) at the Advanced Light Source, collected the X-ray data at the BCSB Beamline 5.0.1 that were used to solve the three-dimensional structures of nonstructural protein NSP2. Understanding the functions of proteins that make these compartments could offer an avenue for disrupting virus production. The team published their findings in Proceedings of the National Academy of Sciences.
Using Nature’s Blueprint for Sustainable Indigo Dyeing Process
Indigo has been prized since antiquity for its vibrancy and deep blue hue and, for more than a century, its unique properties have been leveraged to produce the popular textile blue denim. However, the dyeing process requires chemical steps that are environmentally damaging. A team of researchers in the Molecular Biophysics and Integrated Bioimaging (MBIB) and Biological Systems and Engineering (BSE) Divisions, at JBEI, and UC Berkeley have developed a promising sustainable indigo dyeing process that relies on genetically engineered bacteria, mimicking the natural biochemical protecting group strategy employed by the Japanese indigo plant Polygonum tinctorium.
Crystallization Screen Created by Berkeley Lab Biosciences Scientists Reaches the Market
X-ray crystallography has been the most successful technique used to solve macromolecular structures, contributing several thousand new entries to the Protein Data Bank (PDB) every year. The protein crystal is the critical starting point for X-ray data collection, and consequently, its properties are correlated with the quality of the data and the level of detail that can be extracted for a macromolecular structure. However, proteins require solutions of specific composition to form crystals for structure determination studies. These specifications are usually determined from exposing the protein to several different solutions in a crystallization screen.
A team of researchers in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division led by Paul Adams and Jose Henrique Pereira have developed a new crystal screen, the Berkeley Screen, with 96 conditions proven to be highly effective at producing crystals for structural determination. The Berkeley Screen is now available to the wider crystallography community commercially.
DOE Under Secretary for Science Paul Dabbar Visits Biosciences Area
Paul Dabbar, Department of Energy’s Under Secretary for Science, visited Berkeley Lab on January 18. The visit focused namely on the Lab’s industry engagement programs. During the visit, Dabbar heard presentations by Mary Maxon, Associate Lab Director for Biosciences, and Blake Simmons, Division Director for Biological Systems and Engineering. Paul Adams, Division Director for Molecular Biophysics & Integrated Bioimaging welcomed Dabbar at the Advanced Light Source, and Todd Pray, Program Head of the Advanced Biofuels and Bioproducts Development Unit gave a tours of its facilities. The visit also included tours of the Integrative Genomics Building construction site and the Joint Bioenergy Institute.
NIH Awards $6.5 Million for Augmenting Structural Biology Research Experience
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.
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