Prof. John A. Tainer trained in X-ray crystallography, biochemistry, and computation. With this foundation, he contributed to structural biochemistry for the biology for DNA repair, reactive oxygen control, the immune response, and other stress responses for >20 years. His NCI-funded papers report robust structural and biophysical measurements to advance understanding of cellular stress responses that are evolutionarily conserved and important in preserving genome stability and preventing diseases in humans. His methods, results, and concepts have stood the test of time: they are often used and cited >30,000 total times.At Scripps, Prof. Tainer created and ran the Scripps NSF Computational Center for Macromolecular Structure along with an NIH P01 on Metalloprotein Structure and Design. He also helped develop and utilize the Scripps share of the NSF San Diego Supercomputer Center. At LBL, he developed and directed the ~$2.9 million/year DOE Program “Molecular Assemblies Genes and Genomics Integrated Efficiently” (MAGGIE) from 2004-2011.At Berkeley, Prof. Tainer designed, developed, and directed the world’s only dual endstation synchrotron beamline SIBYLS (Structurally Integrated BiologY for Life Sciences), used by >200 NIH labs. This unique technology integrates high flux small angle x-ray scattering (SAXS) and macromolecular X-ray crystallography (MX). At SIBYLS his lab develop, optimize, and apply technologies to determine accurate structures, conformations and assemblies both in solution and at high resolution. His lab defined an R-factor gap in MX revealing an untapped potential for insights on nanoscale structures by better modeling of bound solvent and flexible regions.At the University of Texas MD Anderson Cancer Center, Prof. Tainer is joining biochemistry and biophysics to fluorescent imaging measures of protein and RNA interactions on DNA for mechanistic insights. He is integrating these data with cryo-EM, MX and SAXS structures by linking MD Anderson and SIBYLS facilities.As an originator of applying proteins from thermophiles to defining dynamic structures and functional conformations, Prof. Tainer develop methods for measurements on structures including conformations, and assemblies in solution. Prof. Tainer has combined cryo-EM and X-ray structures with biochemistry to define functional assemblies. His lab introduced new equations for analyzing X-ray scattering for flexible macromolecules and complexes. His lab also defined a novel SAXS invariant: the first discovered since the Porod invariant ~60 years ago. The defined parameters quantitatively assess flexibility, measure intermolecular distances, determine data to model agreement, and reduce false positives.Prof. Tainer has a track record of successful collaborations, completing projects, sharing innovating approaches and technologies, developing insights along with new structural data, and providing fundamentally important technologies that improve the ways others do their research. He has benefited from continuous peer-reviewed NCI funding since 1999. NCI support has allowed Prof. Tainer to develop expertise in the methods development and in the structural biology of DNA repair, immune responses, and other stress.

• 1. SAXS foundations and metricsRobert Rambo2. Contrast variation sample preparation protocols, experimental procedures, and rudimentary analysisLois Pollack3. Molecular deuteration for neutron scatteringAnthony Patrick Duff4. Planning, Executing and Assessing the Feasibility of SANS Contrast Variation ExperimentsSusan Krueger5. Technical considerations for small-angle neutron scattering from biological macromoleculesCy Jeffries and Andrew Whitten6. Advanced sample environments and capabilities at our synchrotron X-ray beamline with example applicationsMelissa Graewert and Dmitri Svergun7. SEC-SAXS-MALS data acquisition and processing pipeline at SIBYLSDaniel Rosenberg and Michal Hammel8. SEC-SAXS: pros and cons, experimental set-up, examples and software developmentsPatrice Vachette, Javier Perez and Aurelien Thureau9. Radiation damage and sample economy for stopped-flow methods in the time regime of millisecond and aboveMichael Weiss10. Stopped-flow-time-resolved SAXSHenning Tidow and Inokentijs Josts11. Insights on Temp-jump, time-resolved SAXSPhilip Anfinrud12. Time-resolved Small-Angle Neutron Scattering (TR-SANS) for structural biology of dynamic systems: history, recent developments, and practical guidelinesFrank Gabel13. SAXS data collection for Protein FibrillationBente Vestergaard and Annette Langkilde14. Actin assemblyKristina Djinovic Carugo15. SAS induced disulfide bond damageEdward Snell16. High pressure SAXSRichard Gillilan17. Challenges and opportunities in soft X-ray scattering of biological moleculesEsther W. Gomez18. Collection of scattering data from lipid membranes and nanodiscsLin Yang19. SANS stealth methods for membrane proteinsHenning Tidow and Inokentijs Josts20. Predicting solution scattering patterns with explicit-solvent molecular simulationsJochen S. Hub21. From dilute to concentrated solutions of intrinsically disordered proteins: Sample preparation and data collectionMarie Skepo22. Extracting physically-relevant ensemble properties of disordered proteins and other polymers from SAXS dataJoshua A. Riback23. Determining topological structures of RNA using SAXSYun Xing Wang24. SAS data analyses of polydisperse systems with special emphasis on transient complexesPau Bernado and Aamin Sagar25. FEL samples and data collectionPeter Zwart

Prof. John A. Tainer trained in X-ray crystallography, biochemistry, and computation. With this foundation, he contributed to structural biochemistry for the biology for DNA repair, reactive oxygen control, the immune response, and other stress responses for >20 years. His NCI-funded papers report robust structural and biophysical measurements to advance understanding of cellular stress responses that are evolutionarily conserved and important in preserving genome stability and preventing diseases in humans. His methods, results, and concepts have stood the test of time: they are often used and cited >30,000 total times.At Scripps, Prof. Tainer created and ran the Scripps NSF Computational Center for Macromolecular Structure along with an NIH P01 on Metalloprotein Structure and Design. He also helped develop and utilize the Scripps share of the NSF San Diego Supercomputer Center. At LBL, he developed and directed the ~$2.9 million/year DOE Program “Molecular Assemblies Genes and Genomics Integrated Efficiently” (MAGGIE) from 2004-2011.At Berkeley, Prof. Tainer designed, developed, and directed the world’s only dual endstation synchrotron beamline SIBYLS (Structurally Integrated BiologY for Life Sciences), used by >200 NIH labs. This unique technology integrates high flux small angle x-ray scattering (SAXS) and macromolecular X-ray crystallography (MX). At SIBYLS his lab develop, optimize, and apply technologies to determine accurate structures, conformations and assemblies both in solution and at high resolution. His lab defined an R-factor gap in MX revealing an untapped potential for insights on nanoscale structures by better modeling of bound solvent and flexible regions.At the University of Texas MD Anderson Cancer Center, Prof. Tainer is joining biochemistry and biophysics to fluorescent imaging measures of protein and RNA interactions on DNA for mechanistic insights. He is integrating these data with cryo-EM, MX and SAXS structures by linking MD Anderson and SIBYLS facilities.As an originator of applying proteins from thermophiles to defining dynamic structures and functional conformations, Prof. Tainer develop methods for measurements on structures including conformations, and assemblies in solution. Prof. Tainer has combined cryo-EM and X-ray structures with biochemistry to define functional assemblies. His lab introduced new equations for analyzing X-ray scattering for flexible macromolecules and complexes. His lab also defined a novel SAXS invariant: the first discovered since the Porod invariant ~60 years ago. The defined parameters quantitatively assess flexibility, measure intermolecular distances, determine data to model agreement, and reduce false positives.Prof. Tainer has a track record of successful collaborations, completing projects, sharing innovating approaches and technologies, developing insights along with new structural data, and providing fundamentally important technologies that improve the ways others do their research. He has benefited from continuous peer-reviewed NCI funding since 1999. NCI support has allowed Prof. Tainer to develop expertise in the methods development and in the structural biology of DNA repair, immune responses, and other stress.

• 1. SAXS foundations and metricsRobert Rambo2. Contrast variation sample preparation protocols, experimental procedures, and rudimentary analysisLois Pollack3. Molecular deuteration for neutron scatteringAnthony Patrick Duff4. Planning, Executing and Assessing the Feasibility of SANS Contrast Variation ExperimentsSusan Krueger5. Technical considerations for small-angle neutron scattering from biological macromoleculesCy Jeffries and Andrew Whitten6. Advanced sample environments and capabilities at our synchrotron X-ray beamline with example applicationsMelissa Graewert and Dmitri Svergun7. SEC-SAXS-MALS data acquisition and processing pipeline at SIBYLSDaniel Rosenberg and Michal Hammel8. SEC-SAXS: pros and cons, experimental set-up, examples and software developmentsPatrice Vachette, Javier Perez and Aurelien Thureau9. Radiation damage and sample economy for stopped-flow methods in the time regime of millisecond and aboveMichael Weiss10. Stopped-flow-time-resolved SAXSHenning Tidow and Inokentijs Josts11. Insights on Temp-jump, time-resolved SAXSPhilip Anfinrud12. Time-resolved Small-Angle Neutron Scattering (TR-SANS) for structural biology of dynamic systems: history, recent developments, and practical guidelinesFrank Gabel13. SAXS data collection for Protein FibrillationBente Vestergaard and Annette Langkilde14. Actin assemblyKristina Djinovic Carugo15. SAS induced disulfide bond damageEdward Snell16. High pressure SAXSRichard Gillilan17. Challenges and opportunities in soft X-ray scattering of biological moleculesEsther W. Gomez18. Collection of scattering data from lipid membranes and nanodiscsLin Yang19. SANS stealth methods for membrane proteinsHenning Tidow and Inokentijs Josts20. Predicting solution scattering patterns with explicit-solvent molecular simulationsJochen S. Hub21. From dilute to concentrated solutions of intrinsically disordered proteins: Sample preparation and data collectionMarie Skepo22. Extracting physically-relevant ensemble properties of disordered proteins and other polymers from SAXS dataJoshua A. Riback23. Determining topological structures of RNA using SAXSYun Xing Wang24. SAS data analyses of polydisperse systems with special emphasis on transient complexesPau Bernado and Aamin Sagar25. FEL samples and data collectionPeter Zwart