Structure
Volume 11, Issue 2, February 2003, Pages 139-145
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Notes from the bench
Dehydration Converts DsbG Crystal Diffraction from Low to High Resolution

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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 Å resolution. After dehydration, there is a spectacular improvement, with the diffraction pattern extending to 2 Å 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.

Keywords

crystal dehydration
X-ray diffraction
Dsb proteins
disulfide isomerase

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