The crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase provides new insights into the mechanism of the regulation of the activity of the pyruvate dehydrogenase complex. Read more »
ALS Work Using Protein Crystallography
Protein crystallography is used for determining the molecular structure of proteins. Crystallized protein molecules cause a beam of incident x-rays to scatter in many directions, with constructive and destructive interference generating a diffraction pattern. By analyzing these patterns, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and thus determine the protein's structure.
Study Gains New Insight Into Bacterial DNA Packing
When bacteria are put in different environments, their genes start to adapt remarkably quickly because the proteins making up their chromosomes can pack and unpack rapidly. Researchers have now imaged this process at the molecular level, a discovery that could eventually enable scientists to develop strategies to control microbial behavior. 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 »
X-ray Crystal Structures of the Influenza M2 Proton Channel Drug-Resistant V27A Mutant Bound to a Spiro-Adamantyl Amine Inhibitor Reveal the Mechanism of Adamantane Resistance
The M2 proton channel, shown with front and back monomer helices removed, is an anti-influenza drug target. Here, a bound inhibitor blocks the transport of protons through the V27A mutant channel. Read more »
ALS Reveals Vulnerability in Cancer-Causing Protein
A promising anticancer drug, AMG 510, was developed by Amgen Inc. with the help of novel structural insights gained from protein structures solved at the ALS. AMG 510, which is currently in phase II clinical trials for efficacy, targets tumors caused by mutations in the KRAS protein, one of the most common causes of cancer. Read more » 
77Se NMR Probes the Protein Environment of Selenomethionine
Sulfur is critical for protein structure and function but lacks a sensitive isotope for nuclear magnetic resonance (NMR) experiments. This can be circumvented by substituting sulfur with selenium, which has an NMR-compatible isotope (77Se). To enable interpretation of the NMR data, the structures of five of protein variants were solved by x-ray crystallography to a resolution of 1.2 Å. Read more »
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