Dehydration converts DsbG crystal diffraction from low to high resolution.
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.
Heras
Begoña
B
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
MA
Byriel
Karl A
KA
Jones
Alun
A
Raina
Satish
S
Martin
Jennifer L
JL
D018360:Crystallography, X-Ray; D003890:Desiccation; D029968:Escherichia coli Proteins / Q000737:chemistry*; D005990:Glycerol / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry*; D033903:Periplasmic Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; D014867:Water; D010088:Oxidoreductases; C109831:DsbG protein, E coli; D005990:Glycerol