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Synchrotron X-ray reciprocal-space mapping, topography and diffraction resolution studies of macromolecular crystal quality

  • T. J. Boggon
  • , J. R. Helliwell
  • , R. A. Judge
  • , A. Olczak
  • , D. P. Siddons
  • , E. H. Snell
  • , V. Stojanoff
  • University of Manchester
  • Icahn School of Medicine at Mount Sinai
  • National Aeronautics and Space Administration
  • Brookhaven National Laboratory
  • European Synchrotron Radiation Facility

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

Abstract

A comprehensive study of microgravity and ground-grown chicken egg-white lysozyme crystals is presented using synchrotron X-ray reciprocal-space mapping, topography techniques and diffraction resolution. Microgravity crystals displayed reduced intrinsic mosaicities on average, but no differences in terms of strain over their ground-grown counterparts. Topographic analysis revealed that in the microgravity case the majority of the crystal was contributing to the peak of the reflection at the appropriate Bragg angle. In the ground-control case only a small volume of the crystal contributed to the intensity at the diffraction peak. The techniques prove to be highly complementary, with the reciprocal-space mapping providing a quantitative measure of the crystal mosaicity and strain (or variation in lattice spacing) and the topography providing a qualitative overall assessment of the crystal in terms of its X-ray diffraction properties. Structural data collection was also carried out at the synchrotron.

Original languageEnglish
Pages (from-to)868-880
Number of pages13
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number7
DOIs
StatePublished - 2000

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