Biosciences Area

Breakthrough in Membrane-Protein Design Settles Long-Standing Debate

Membrane proteins that connect a cell’s inner workings with the outside world are essential for life and genetic mutations that affect their structural integrity or biological function are the cause of many diseases. Given their importance, researchers are interested in ascertaining the general physics principles underlying how membrane proteins fold and stabilize their molecular structures. Using high-resolution protein crystallography at the Advanced Light Source (ALS) Beamline 8.3.1, scientists from UCSF characterized designed membrane proteins to better understand the forces that stabilize these large, complex structures.

Read the ALS Science Highlight.

SIBYLS Sheds Light on Enzyme that Regulates Blood-clotting Factor

A group of researchers at Washington University School of Medicine have used the capabilities available at the Advanced Light Source’s SIBYLS beamline to gain insight into an enzyme that functions in blood clotting. ADAMTS13, which stands for a disintegrin and metalloproteinase with thrombospondin-1 repeats, member 13, is a multi-domain protease enzyme whose catalytic mechanism involves a metal. It is the only known protein to regulate the adhesive function of von Willebrand factor (VWF), a blood clotting protein involved in hemostasis.

BCSB Helps Elucidate Mechanism of Innate Immune Response

The crystallographic study of STING (stimulator of interferon genes), a transmembrane protein that plays a key role in innate immunity, in complex with TBK1 (serine/threonine-protein kinase), an enzyme that regulates the inflammatory response to foreign DNA, is extremely challenging due to weakly diffracting crystals. But thanks to the expertise of Berkeley Center for Structural Biology (BCSB) scientists, researchers from Texas A&M University (TAMU) were able to pinpoint the conserved motif of STING that mediates the recruitment and activation of TBK1. They published their results in Nature.

Antibody Uses Mimicry to Block SARS Coronavirus

To better understand how coronavirus antibodies work, a team of researchers at the University of Washington studied spike protein structures in complex with neutralizing antibody fragments isolated from SARS and MERS survivors. To visualize how the spike structures interact with the antibody fragments, they used a cryo-electron microscopy (cryo-EM) for the spikes, which are resistant to crystallization, and protein crystallography for the fragments. The high-resolution x-ray crystallography was performed at the Advanced Light Source (ALS) Beamline 5.0.1, part of the Berkeley Center for Structural Biology (BCSB).

BCSB Helps Characterize New Arsenic-based Antibiotic

A newly-discovered arsenic-containing compound produced by a soil bacterium shows promise as a broad-spectrum antibiotic. In a paper published in the Nature journal Communications Biology, an international team of researchers demonstrated that arsinothricin (AST) is effective against many types of gram-negative and gram-positive bacteria. The effort was led by Barry Rosen of the Florida International University College of Medicine and Masafumi Yoshinaga of the National Agriculture and Food Research Organization (NARO) in Japan. Banumathi Sankaran, a research scientist in the Berkeley Center for Structural Biology (BSCB) at the Advanced Light Source (ALS), was an author on the paper.

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