Science Highlights

Protein flexibility linked to severity of Lou Gerhig’s disease

SAXS and MX data collected at SIBYLS enabled insights into protein flexibility in one of the proteins involved in Lou Gerigh’s disease. The results were recently published in PNAS and have been highlighted by [Today At Berkeley Lab](http://newscenter.lbl.gov/2014/10/13/berkeley-lab-and-scripps-research-institute-scientists-link-als-progression-to-increased-protein-instability/) and and [Daily Cal](http://www.dailycal.org/2014/10/16/berkeley-lab-scripps-institute-propose-cause-als/). >Protein framework alterations in heritable Cu, Zn superoxide dismutase (SOD) mutants cause misassembly…
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SAXS and EM used to determine structure of Gold Nanopartice

Recently in Science: >Structure determination of gold nanoparticles (AuNPs) is necessary for understanding their physical and chemical properties, but only one AuNP larger than 1 nanometer in diameter [a 102-gold atom NP (Au102NP)] has been solved to atomic resolution. Whereas the Au102NP structure was determined by x-ray crystallography, other large AuNPs have proved refractory to…
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Practical High-throughput SAXS

A new publication is available that describes practical aspects of collecting High-throughput SAXS data at the SIBYLS beamline, with a focus on challenging low concentration samples. Additional practical advice is laid out with respect to interpreting the resulting data. Dyer KN, Hammel M, Rambo RP, Tsutakawa SE, Rodic I, Classen S, Tainer JA, Hura GL.…
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How a Shape-shifting DNA-repair Machine Fights Cancer

The SIBYLS beamline was instrumental in providing key structural data for two recent publications exploring the dynamic nature of DNA repair. >The Mre11‐Rad50 complex is highly conserved, yet the mechanisms by which Rad50 ATP‐driven states regulate the sensing, processing and signaling of DNA double‐strand breaks are largely unknown. Here we design structure‐based mutations in Pyrococcus…
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Nanogold labels used to characterize DNA bending in mismatch repair

Greg Hura and colleagues developed and applied nanogold labels for DNA complexes with proteins examined by small angle X-ray scattering (SAXS) to follow DNA conformations acting in error detection by the mismatch repair (MMR) system in solution. This technique can examine short or long pieces of DNA and in most solution conditions, including those closest…
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New crystal structures of translocating ribosome

Several new crystal structures of the 70S ribosome in complex with EFG and non-hydrolyzable GTP analogs have revealed how the ribosome directionally translocates mRNA and the tRNAs through the A, P, and E sites and how specific features of EFG and ribosomal RNA act as pawls to enforce this ratcheting mechanism. The new structures were…
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Comprehensive macromolecular conformations mapped by quantitative SAXS analyses

SIBYLS scientists have recently published and made available tools for generating [SAXS structural comparison maps](/saxs_similarity “SAXS structural comparison maps”). Details of the methods have been published in Nature Methods. >Biological macromolecular functions require distinct conformational states that are challenging to examine comprehensively. Current methods to quantify conformational similarities and distinguish different assembly states are underdeveloped.…
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Super-Resolution in Solution X-Ray Scattering and Its Applications to Structural Systems Biology

Rob and John have a new review on SAXS and its application to systems biology published in the Annual Review of Biophysics. See if you can spot the musical theme. >Small-angle X-ray scattering (SAXS) is a robust technique for the comprehensive structural characterizations of biological macromolecular complexes in solution. Here, we present a coherent synthesis…
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