Chapter 19.3 Small-angle X-ray scattering

Crystallography of biological macromolecules

First Online Edition (2006)

Part 19. Other experimental techniques

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

Published Online: 1 JAN 2006

DOI: 10.1107/97809553602060000700

International Tables for Crystallography

International Tables for Crystallography

How to Cite

Tsuruta, H. and Johnson, J. E. 2006. Small-angle X-ray scattering. International Tables for Crystallography. F:19:19.3:428–437.

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: 1 JAN 2006


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