SIBYLS user Tim Stachowski and the Snell group make the cover of the Journal of Synchrotron Radiation for their paper describing their work using Small-angle X-ray Scattering to evaluate how three scavengers commonly used in crystallographic experiments perform in solution at 10°C. In this study, they found the SAXS-based method can detect damage at X-ray doses far lower than those accessible crystallographically, thereby providing a detailed picture of scavenger processes. Their approach provides a platform for more systematic and comprehensive screening of radioprotectants that can directly inform mitigation strategies for both solution and crystallographic experiments, while also clarifying fundamental radiation damage mechanisms.


protein science cover.pngSIBYLS scientists Michal Hammel and John Tainer describe the mechanistic insights into NHEJ structural biochemistry determined by small angle X-ray scattering (SAXS) results combined with X-ray crystallography (MX) and cryo-electron microscopy (cryo-EM).
The cover image, like the old car engine malfunctioning without a linchpin and flexible belt, shows the NHEJ efficiency arises from a flexible conformational control principle. The NHEJ components were matched on the SKODA 100 car engine built in 1973 in Czechoslovakia.


With more than 50 participants and several amazing speakers, this year’s BioSAXS workshop was one of our best workshops to date. If you were not able to attend or if you missed part of it, you can find the recordings on our SIBYLS beamline YouTube channel.

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The 12th annual BioSAXS workshop is just around the corner! Once again, it will be held virtually (via zoom) during the 2021 ALS User Meeting. Join us from the comfort of your home!

Email Kathryn to receive the zoom link

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FINAL 2021 BioSAXS Workshop Schedule (PST).pdf
FINAL 2021 BioSAXS Workshop Schedule (MST).pdf
FINAL 2021 BioSAXS Workshop Schedule (CST).pdf
FINAL 2021 BioSAXS Workshop Schedule (EST).pdf
FINAL 2021 BioSAXS Workshop Schedule (England).pdf
FINAL 2021 BioSAXS Workshop Schedule (Slovakia).pdf


This two-day BioSAXS workshop is designed for current and future SIBYLS SAXS users. The latest advances in SAXS studies on biological systems will be discussed with particular focus on advances in our mail-in SAXS program and on advances in synchrotron scattering techniques, modeling of dynamic and flexible structures, integrating high-resolution models in the SAXS modeling, bioSAXS with membrane protein, and integrating bioSAXS analysis within cryo-EM imaging and crystallography.

On the first day, SIBYLS Lab’s SAXS Beamline Scientists will introduce the future of high throughput and size exclusion coupled SAXS (HT-SAXS and SEC-SAXS). Additionally, we have an exciting group of experienced scientists from around the world who will present talks. Dr. Robert Rambo is the principal beamline scientist at beamline B21 at the Diamond Light Source in Oxford, England. Dr. Rambo is the author of ScÅtter and will expound on using this tool for SAXS analysis. Dr. Nozomi Ando, a principal investigator at Cornell University best known for using X-ray scattering approaches to embrace conformational disorder, will speak about EFA and SVD applications for SAXS.

Other speakers include Dr. Soumya Remesh from the Wells Lab at UCSF. Dr. Remesh will speak on SAXS and SARS-Cov-2 protein. Dr. Aleem Syed from MD Anderson Cancer Center will speak on SAXS and DNA-proteins. Dr. Gundeep Kaur, also from MD Anderson Cancer Center, will give a talk on DNA-protein complexes.

On the second day, we will provide participants with software tutorial sessions for biological SAXS and provide an opportunity for participants to present and discuss their projects with the SIBYLS staff. Interested users will present their case studies for workshop analysis. This will provide for a flux of ideas among workshop participants, and inspire new perspectives for future data analysis.

screenshot 23.png In collaboration with Adrzej Joachimiak of Argonne National Lab, and Hugh M. O’Neill of Oak Ridge National lab (among others), Greg Hura and his team at the SIBYLS beamline determine how components of the SARS-CoV-2 replication mechanism fit together. Using SAXS data collected at SIBYLS along with other approaches, these researchers were able to determine how components of the SARS-CoV-2 replication mechanism fit together. This breakthrough research is the first step toward developing treatments for COVID-19 viral infection.


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By combining SAXS results with MX and cryo-EM, Michal Hammel and John Tainer reviewed mechanistic insights into NHEJ structural bio-chemistry. Integrated structures reveal multifunctional roles for disordered linkers and modular dynamic interfaces promoting DSB end processing and alignment into the short-range complex for ligation by LigIV. Integrated findings define dynamic assemblies fundamental to designing separation-of-function mutants and allosteric inhibitors targeting conformational transitions in multifunctional complexes.


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SIBYLS scientists, Michal Hammel and John Tainer, show that the marriage of SAXS with cryo-EM leverages the strengths of both techniques to enable assessment of functional conformations and flexibility defining atomic-resolution molecular mechanisms for DSB repair. SAXS, which measures thermodynamic solution-state conformational states and assemblies outside of cryo- and solid-state conditions, unveils the inherent flexibility of KU, DNA-PKcs and DNA-PK.


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