Dehydration converts DsbG crystal diffraction from low to high resolution

  • Heras B
  • Edeling M
  • Byriel K
 et al. 
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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.

Author-supplied keywords

  • Crystal dehydration
  • Disulfide isomerase
  • Dsb proteins
  • X-ray diffraction

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  • Begoña Heras

  • Melissa A. Edeling

  • Karl A. Byriel

  • Alun Jones

  • Satish Raina

  • Jennifer L. Martin

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