Crystallographic phasing from weak anomalous signals

Curr Opin Struct Biol. 2015 Oct:34:99-107. doi: 10.1016/j.sbi.2015.08.003. Epub 2015 Sep 30.

Abstract

The exploitation of anomalous signals for biological structural solution is maturing. Single-wavelength anomalous diffraction (SAD) is dominant in de novo structure analysis. Nevertheless, for challenging structures where the resolution is low (dmin≥3.5Å) or where only lighter atoms (Z≤20) are present, as for native macromolecules, solved SAD structures are still scarce. With the recent rapid development in crystal handling, beamline instrumentation, optimization of data collection strategies, use of multiple crystals and structure determination technologies, the weak anomalous diffraction signals are now robustly measured and should be used for routine SAD structure determination. The review covers these recent advances on weak anomalous signals measurement, analysis and utilization.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Crystallization
  • Crystallography, X-Ray / methods*
  • Models, Molecular
  • Molecular Conformation
  • X-Ray Diffraction