Dehydration converts DsbG crystal diffraction from low to high resolution

Structure. 2003 Feb;11(2):139-45. doi: 10.1016/s0969-2126(03)00005-4.

Abstract

Diffraction quality crystals are essential for crystallographic studies of protein structure, and the production of poorly diffracting crystals is often regarded as a dead end in the process. Here we show a dramatic improvement of poorly diffracting DsbG crystals allowing high-resolution diffraction data measurement. Before dehydration, the crystals are fragile and the diffraction pattern is streaky, extending to 10 A resolution. After dehydration, there is a spectacular improvement, with the diffraction pattern extending to 2 A resolution. This and other recent results show that dehydration is a simple, rapid, and inexpensive approach to convert poor quality crystals into diffraction quality crystals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray*
  • Desiccation
  • Escherichia coli Proteins / chemistry*
  • Glycerol / metabolism
  • Oxidoreductases / chemistry*
  • Periplasmic Proteins / chemistry*
  • Water / chemistry

Substances

  • Escherichia coli Proteins
  • Periplasmic Proteins
  • Water
  • Oxidoreductases
  • DsbG protein, E coli
  • Glycerol