Using structural data from the ALS and cryo-electron microscopy, researchers have characterized how an antibody binds to and neutralizes SARS-CoV-2. This work provides the basis for therapeutic and vaccine development for the SARS-CoV-2 virus, which is responsible for the COVID-19 pandemic. Read more »
On-Off Switch for Regulating Tumor-Cell Growth
The mechanisms that affect the regulation of cell growth in certain tumor cells were revealed by a Genentech study of enzyme structures, conducted in part at the ALS. The work establishes a framework for the rational discovery of new therapeutics to improve upon currently existing treatments for certain cancers. Read more »
How a Cancer Drug Targets Proteins for Degradation
Protein structures obtained by Novartis researchers helped reveal how a cancer drug promotes the degradation of proteins essential to cell proliferation. A detailed understanding of the drug’s mechanism of action is key to determining whether the protein-degradation system can be reprogrammed to degrade different targets. Read more »
X-Ray Experiments Zero in on COVID-19 Antibodies
In the fight against SARS-CoV-2, scientists have been working on identifying neutralizing antibodies that could be used in preventative treatments or as post-exposure therapies. The latest findings, which include data from the ALS, indicate that antibodies from SARS survivors could potently block entry of SARS-CoV-2 into host cells. Read more »
Study Leads to Firmer Grasp of Biochemical “Reactive Handle”
Protein crystallography provided new insight into a functional group of molecules that, if added to bacterial enzymes, could enable a variety of alterations to the bacteria’s polymer output. Tweaking enzymes to produce these “reactive handles” is a first step toward biosynthesizing diverse polymers with tailored properties. Read more »
Staff at Berkeley Lab’s X-Ray Facility Mobilize to Support COVID-19-Related Research
X-rays allow researchers to map out the 3D structure of proteins relevant to diseases at the scale of molecules and atoms, and the ALS has been recalled to action to support research related to COVID-19, the coronavirus disease that has already infected about 2 million people around the world. Read more »
Discovery of a Covalent Inhibitor of KRASG12C (AMG 510) for the Treatment of Solid Tumors
KRASG12C has emerged as a promising target in the treatment of solid tumors; however, clinically viable inhibitors have yet to be identified. Here, researchers report on structure-based design and optimization efforts, culminating in the identification of AMG 510, a highly potent, selective, and well-tolerated KRASG12C inhibitor currently in phase I clinical trials (NCT03600883). Read more »
A Citizen-Science Computer Game for Protein Design
Using the computer game, “Foldit,” nonexpert citizen scientists designed new proteins whose structures, verified at the ALS, were equivalent in quality to and more structurally diverse than computer-generated designs. The work shows the potential of using crowd-based creativity in the design of new proteins for fighting illness and disease. Read more » 
X-Ray Experiments Contribute to Studies of a Drug Now Approved to Combat Tuberculosis
The U.S. Food and Drug Administration has approved a new antibiotic that, in combination with two existing antibiotics, can tackle one of the most formidable and deadly treatment-resistant forms of the bacterium that causes tuberculosis. Studies exploring the structure and function of the new drug benefited from x-ray experiments at the ALS. Read more »
X-Ray Studies Key in Study Relating to Immune System-Signaling Protein
A grouping of amino acids—part of an important signaling protein, STING—plays an important role in activating the immune system. A study conducted through the Collaborative Crystallography program at the ALS confirmed how this part of the STING protein helps to bind a protein-modifying enzyme associated with autoimmune diseases and some cancers. Read more »