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

Crystallographic phasing from weak anomalous signals.

Author information

1
New York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA. Electronic address: qunliu@bnl.gov.
2
New York Consortium on Membrane Protein Structure, New York Structural Biology Center, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA. Electronic address: wayne@xtl.cumc.columbia.edu.

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.

PMID:
26432413
PMCID:
PMC4684729
DOI:
10.1016/j.sbi.2015.08.003
[Indexed for MEDLINE]
Free PMC Article

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