title: Dehydration converts DsbG crystal diffraction from low to high resolution.
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.
authors.affiliation: 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.
authors.forename: Begoña
authors.initials: B
authors.lastname: Heras
authors.forename: Melissa A
authors.initials: MA
authors.lastname: Edeling
authors.forename: Karl A
authors.initials: KA
authors.lastname: Byriel
authors.forename: Alun
authors.initials: A
authors.lastname: Jones
authors.forename: Satish
authors.initials: S
authors.lastname: Raina
authors.forename: Jennifer L
authors.initials: JL
authors.lastname: Martin
mesh_terms: 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
chemical_list: D029968:Escherichia coli Proteins; D033903:Periplasmic Proteins; D014867:Water; D010088:Oxidoreductases; C109831:DsbG protein, E coli; D005990:Glycerol