title: Improving diffraction resolution using a new dehydration method.
abstract: The production of high-quality crystals is one of the major obstacles in determining the three-dimensional structure of macromolecules by X-ray crystallography. It is fairly common that a visually well formed crystal diffracts poorly to a resolution that is too low to be suitable for structure determination. Dehydration has proven to be an effective post-crystallization treatment for improving crystal diffraction quality. Several dehydration methods have been developed, but no single one of them is suitable for all crystals. Here, a new convenient and effective dehydration method is reported that makes use of a dehydrating solution that will not dry out in air for several hours. Using this dehydration method, the resolution of Archaeoglobus fulgidus Cas5a crystals has been increased from 3.2 to 1.95 Å and the resolution of Escherichia coli LptA crystals has been increased from <5 to 3.4 Å.
authors: MacCHESS, Cornell University, Ithaca, NY 14853, USA.
authors: Qingqiu
authors: Q
authors: Huang
authors: MacCHESS, Cornell University, Ithaca, NY 14853, USA.
authors: Doletha M E
authors: DM
authors: Szebenyi
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry*; D019611:Archaeoglobus fulgidus / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D003681:Dehydration; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D019843:Archaeal Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C532155:LptA protein, E coli
keywords: Cas5a; LptA; dehydration; diffraction resolution; protein crystal