Feasibility of one-shot-per-crystal structure determination using Laue diffraction

Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):2-11. doi: 10.1107/S0907444909037731. Epub 2009 Dec 21.

Abstract

Crystal size is an important factor in determining the number of diffraction patterns which may be obtained from a protein crystal before severe radiation damage sets in. As crystal dimensions decrease this number is reduced, eventually falling to one, at which point a complete data set must be assembled using data from multiple crystals. When only a single exposure is to be collected from each crystal, the polychromatic Laue technique may be preferable to monochromatic methods owing to its simultaneous recording of a large number of fully recorded reflections per image. To assess the feasibility of solving structures using single Laue images from multiple crystals, data were collected using a 'pink' beam at the CHESS D1 station from groups of lysozyme crystals with dimensions of the order of 20-30 microm mounted on MicroMesh grids. Single-shot Laue data were used for structure determination by molecular replacement and correct solutions were obtained even when as few as five crystals were used.

Publication types

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

MeSH terms

  • Animals
  • Chickens
  • Crystallization
  • Crystallography, X-Ray / instrumentation
  • Crystallography, X-Ray / methods*
  • Feasibility Studies
  • Muramidase / chemistry*
  • Muramidase / metabolism
  • Protein Conformation

Substances

  • Muramidase