Chapter 19.3 Small‐angle X‐ray scattering

Crystallography of biological macromolecules

Second Online Edition (2012)

Part 19. Other experimental techniques

  1. H. Tsuruta1,
  2. J. E. Johnson2

Published Online: 14 APR 2012

DOI: 10.1107/97809553602060000869

International Tables for Crystallography

International Tables for Crystallography

How to Cite

Tsuruta, H. and Johnson, J. E. 2012. Small‐angle X‐ray scattering. International Tables for Crystallography. F:19:19.3:563–574.

Author Information

  1. 1

    SSRL/SLAC & Department of Chemistry, Stanford University, PO Box 4349, MS69, Stanford, California 94309–0210, USA

  2. 2

    Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA

Publication History

  1. Published Online: 14 APR 2012



Small‐angle X‐ray scattering (SAXS) has emerged as an important method for studying large‐scale dynamic processes, ranging from protein folding to virus particle polymorphism. The renaissance of this method has resulted from a variety of advances in molecular biology and X‐ray instrumentation, and these have dramatically increased the information content of the derived results. Modern synchrotron X‐ray sources and advanced detector systems have lead to higher‐resolution data in both the spatial and time domains. The purpose of this chapter is to address practical aspects of SAXS as they relate to and complement macromolecular crystallography.


  • data collection;
  • data processing;
  • protein folding;
  • small‐angle X‐ray scattering;
  • solution X‐ray scattering;
  • synchrotron radiation;
  • time‐resolved studies