Academic Press Small Angle Scattering Part A: Methods for Structural Investigation (Volume 677) (Methods in Enzymology, Volume 677)

Small Angle Scattering, Part A: Methods for Structural Investigation, Volume 674 in the Methods in Enzymology series, highlights new advances in the field, with new chapters in this updated release including SAXS foundations and metrics, Contrast variation sample preparation protocols, experimental procedures, and rudimentary analysis, Molecular deuteration for neutron scattering, Planning, Executing and Assessing the Feasibility of SANS Contrast Variation Experiments, Technical considerations for small-angle neutron scattering from biological macromolecules, and Advanced sample environments and capabilities at our synchrotron X-ray beamline with example applications. Additional sections in the book cover SEC-SAXS-MALS data acquisition and processing pipeline at SIBYLS, SEC-SAXS: pros and cons, experimental set-up, examples and software developments, Radiation damage and sample economy for stopped-flow methods in the time regime of millisecond and above, Stopped-flow-time-resolved SAXS, Insights on Temp-jump, time-resolved SAXS, and much more. Review Edited by some of the best scientists in the field, this series presents the latest updates in the field of enzymology About the Author 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