title: Structural Analysis of the Flagellar Component Proteins in Solution by Small Angle X-Ray Scattering.
abstract: Small angle X-ray scattering is an increasingly utilized method for characterizing the shape and structural properties of proteins in solution. The technique is amenable to very large protein complexes and to dynamic particles with different conformational states. It is therefore ideally suited to the analysis of some flagellar motor components. Indeed, we recently used the method to analyze the solution structure of the flagellar motor protein FliG, which when combined with high-resolution snapshots of conformational states from crystal structures, led to insights into conformational transitions that are important in mediating the self-assembly of the bacterial flagellar motor. Here, we describe procedures for X-ray scattering data collection of flagellar motor components, data analysis, and interpretation.
authors.affiliation: European Molecular Biology Laboratory Australia Node for Single Molecule Science, School of Medical Sciences, University of New South Wales, Sydney, NSW, Australia. lawrence.lee@unsw.edu.au.|Structural and Computational Biology Division, Victor Chang Cardiac Research Institute, Darlinghurst, NSW, Australia. lawrence.lee@unsw.edu.au.
authors.forename: Lawrence K
authors.initials: LK
authors.lastname: Lee
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods; D005407:Flagella / Q000737:chemistry*; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction / Q000379:methods; D014965:X-Rays
chemical_list: D001426:Bacterial Proteins
keywords: Bacterial flagellar motor; Chemotaxis; Motility; Protein dynamics; Protein structure; Small angle X-ray scattering; Synchrotron radiation