Processing incommensurately modulated protein diffraction data with Eval15

Jason Porta, Jeffrey J. Lovelace, Antoine M.M. Schreurs, Loes M.J. Kroon-Batenburg, Gloria E.O. Borgstahl

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Recent challenges in biological X-ray crystallography include the processing of modulated diffraction data. A modulated crystal has lost its three-dimensional translational symmetry but retains long-range order that can be restored by refining a periodic modulation function. The presence of a crystal modulation is indicated by an X-ray diffraction pattern with periodic main reflections flanked by off-lattice satellite reflections. While the periodic main reflections can easily be indexed using three reciprocal-lattice vectors a*, b*, c*, the satellite reflections have a non-integral relationship to the main lattice and require a q vector for indexing. While methods for the processing of diffraction intensities from modulated small-molecule crystals are well developed, they have not been applied in protein crystallography. A recipe is presented here for processing incommensurately modulated data from a macromolecular crystal using the Eval program suite. The diffraction data are from an incommensurately modulated crystal of profilin-actin with single-order satellites parallel to b*. The steps taken in this report can be used as a guide for protein crystallographers when encountering crystal modulations. To our knowledge, this is the first report of the processing of data from an incommensurately modulated macromolecular crystal.

Original languageEnglish (US)
Pages (from-to)628-638
Number of pages11
JournalActa Crystallographica Section D: Biological Crystallography
Volume67
Issue number7
DOIs
StatePublished - Jul 1 2011

Keywords

  • Eval15
  • incommensurate
  • modulation
  • profilin-actin

ASJC Scopus subject areas

  • Structural Biology

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