CASP is the Critical Assessment of Protein Structure Predictions, a biannual “competition” to determine which prediction algorithm generates the most accurate model. There are several categories in which models will be assessed, including accuracy, topology, and biological relevance. The SIBYLS beamline is participating to provide small-angle X-ray scattering (SAXS) data for––and judging for the first time––the “data-assisted” category. This CASP competition should lead to improvement in predicting protein-protein interfaces and complex structures.
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.
A Hollow Pyramid Unlocks Principles of Protein Architecture
Researchers at UCLA have designed a hollow, pyramid-shaped protein with a controllable cavity size that may aid the capture and release of smaller compounds. The tools used in this work, including small angle X-ray scattering techniques at the SIBYLS beamline in the Advanced Light Source (ALS), will help analyze and optimize designed-protein assemblies and understand their behavior in solution. Read more in the ALS Science Brief.
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.
Unexpected Key Role for Unfolded Protein Regions in DNA Break Repair Defined
Structurally Integrated Biology for Life Sciences (SIBYLS) beamline researchers, led by research scientist Michal Hammel of the Molecular Biophysics & Integrated Bioimaging (MBIB) Division, used X-ray scattering to define an unexpected key role for unfolded protein regions in DNA break repair to allow regulation plus access to DNA ends. The concept of DNA break repair as a flexibly-linked dynamic complex, as opposed to a linear pathway, suggests new approaches to targeting DNA repair for selectively killing cancer cells due to their high levels of DNA instability. Their findings were published in a recent cover article of the Journal of Biological Chemistry.
The SIBYLS beamline of the Advanced Light Source at Berkeley Lab, directed by MBIB’s senior scientist John Tainer, is optimized for both small-angle X-ray scattering (SAXS) and macromolecular crystallography (MX), making it unique among the world’s mostly SAXS or MX dedicated beamlines.
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