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

J Struct Biol. 2010 Oct;172(1):128-41. doi: 10.1016/j.jsb.2010.06.012. Epub 2010 Jun 15.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Models, Molecular
  • Multiprotein Complexes / chemistry*
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Proteins / chemistry*
  • Scattering, Small Angle*
  • Solutions
  • X-Ray Diffraction / methods*

Substances

  • Multiprotein Complexes
  • Proteins
  • Solutions