4.4 Article

Structural characterization of proteins and complexes using small-angle X-ray solution scattering

Journal

JOURNAL OF STRUCTURAL BIOLOGY
Volume 172, Issue 1, Pages 128-141

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2010.06.012

Keywords

Small-angle scattering; Solution scattering; Macromolecular structure; Functional complexes; Ab initio methods; Rigid body modeling; Flexible macromolecules

Funding

  1. HFSP [RGP0055/2006-C]
  2. EMBL

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Small-angle scattering of X-rays (SAXS) is an established method for the low-resolution structural characterization of biological macromolecules in solution. The technique provides three-dimensional low-resolution structures, using ab initio and rigid body modeling, and allow one to assess the oligomeric state of proteins and protein complexes. In addition, SAXS is a powerful tool for structure validation and the quantitative analysis of flexible systems, and is highly complementary to the high resolution methods of X-ray crystallography and NMR. At present, SAXS analysis methods have reached an advanced state, allowing for automated and rapid characterization of protein solutions in terms of low-resolution models, quaternary structure and oligomeric composition. In this communication, main approaches to the characterization of proteins and protein complexes using SAXS are reviewed. The tools for the analysis of proteins in solution are presented, and the impact that these tools have made in modern structural biology is discussed. (C) 2010 Elsevier Inc. All rights reserved.

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