The complimentary use of small angle x-ray scattering with crystallography in the determination of biological macromolecular structures

Project_Goals: Recent advances in small angle x-ray scattering (SAXS) technique and analysis have enabled shape prediction of proteins in solution. The SAXS technique is particularly powerful in combination with partial high resolution structures. SAXS can efficiently reveal the spatial organization of protein domains, including domains missing from or disordered in known crystal structures, and establish cofactor or substrate-induced conformational changes. Following a short introduction to SAXS, examples from data collected at SIBYLS, a dual SAXS and protein crystallography synchrotron beamline, will be drawn upon to demonstrate the complimentary use of SAXS with protein crystallography. I will also describe the recent implementation of a sample loading automation tool for true high throughput SAXS data collection. Several examples of the utility of high throughput SAXS will discussed in the context of the DOE/Gtl funded program project MAGGIE (Molecular Assemblies, Genes, and Genomics Integrated Efficiently).