A critical component of the planned state-of-the-art macromolecular crystallography beamline Gemini has arrived at the Lab. The specially-designed in-vacuum undulator insertion device will yield higher photon flux compared to the Advanced Light Source’s superbend magnet and wiggler sources, bringing solutions to some of the most challenging projects in structural biology within reach.
ALS Passes the 7000-Protein Milestone
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.
Modified Antibody Clarifies Tumor-Killing Mechanisms
At the Advanced Light Source (ALS), researchers studied an antibody that was modified to activate a specific pathway of the immune system, demonstrating its value in killing tumor cells. The work provides a platform for disentangling the effects of different immune-system pathways and could lead to the design of improved cancer immunotherapies. The protein crystallography data in the study, which showed how an extreme twist in the modified antibody structure led to its selectivity, was collected at ALS Beamline 5.0.3 , which is part of the Biosciences’ Berkeley Center for Structural Biology; and at the Advanced Photon Source. Go to the ALS website to learn more.
Designing Cyclic Oligomers: Greater than the Sum of Their Parts
Cyclic proteins that assemble from multiple identical subunits (homo-oligomers) play key roles in many biological processes, including enzymatic catalysis and function and cell signaling. Researchers in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division worked with University of Washington’s David Baker, who led a team to design in silico and crystallize self-assembling cyclic homo-oligomer proteins.
Researchers Gain Insight into Protein Critical to Zika Virus Reproduction
Zika virus is a mosquito-borne infectious disease linked to certain birth defects in infants in South and Central America and the United States. A Lawrence Berkeley National Laboratory (Berkeley Lab) researcher, Banumathi Sankaran, worked as part of a multi-institutional team led by Cheng Kao, professor at Indiana University, and Pingwei Li, associate professor at Texas A&M University (TAMU), to map a key viral protein called NS5. Necessary to virus reproduction, NS5 contains two enzyme activities: one reduces the body’s ability to mount an immune response against infection and the other helps start the genetic replication process.
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