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PMID: 12575933 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Dehydration converts DsbG crystal diffraction from low to high resolution.

Structure (London, England : 1993) ·Vol. 11 ·No. 2 ·2003-02-00 ·Pages 139-45

Heras B, Edeling MA, Byriel KA, Jones A, Raina S, Martin JL

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.

MeSH Terms
Crystallography, X-Ray Desiccation Escherichia coli Proteins/chemistry Glycerol/metabolism Oxidoreductases/chemistry Periplasmic Proteins/chemistry Water/chemistry
Chemicals
Escherichia coli Proteins Periplasmic Proteins Water Oxidoreductases DsbG protein, E coli Glycerol
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Heras Begoña
Centre for Drug Design and Development and Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience, University of Queensland, QLD 4072, Brisbane, Australia.
Edeling Melissa A
Byriel Karl A
Jones Alun
Raina Satish
Martin Jennifer L
Article Info
Journal
Structure (London, England : 1993)
Abbr.
Structure
ISSN
0969-2126
Published
2003-02-00
Pages
139-45
Language
English
Region
United States
NLM ID
101087697
Subset
IM
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