Coherent X-ray diffractive imaging of protein crystals

J Synchrotron Radiat. 2008 Nov;15(Pt 6):576-83. doi: 10.1107/S0909049508029439. Epub 2008 Oct 3.

Abstract

The technique of coherent X-ray diffraction imaging (CXDI) has recently shown great promise for the study of inorganic nanocrystals. In this work the CXDI method has been applied to the study of micrometer-size protein crystals. Finely sampled diffraction patterns of single crystals were measured and iterative phase-retrieval algorithms were used to reconstruct the two-dimensional shape of the crystal. The density maps have limited reproducibility because of radiation damage, but show clear evidence for crystal facets. Qualitative analysis of a number of single-crystal diffraction peaks indicates the presence of inward surface contraction on 2 microm size crystals. A survey of several hundred diffraction patterns yielded a number of examples with dramatic single-sided streaks, for which a plausible model is constructed.

Publication types

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

MeSH terms

  • Algorithms*
  • Crystallization
  • Crystallography, X-Ray / methods
  • Image Interpretation, Computer-Assisted / methods*
  • Proteins / chemistry*
  • Proteins / ultrastructure*
  • Tomography, Optical Coherence / methods*
  • X-Ray Diffraction / methods*

Substances

  • Proteins