title: Measurement of the intrinsic variability within protein crystals: implications for sample-evaluation and data-collection strategies.
abstract: The advent of micro-focused X-ray beams has led to the development of a number of advanced methods of sample evaluation and data collection. In particular, multiple-position data-collection and helical oscillation strategies are now becoming commonplace in order to alleviate the problems associated with radiation damage. However, intra-crystal and inter-crystal variation means that it is not always obvious on which crystals or on which region or regions of a crystal these protocols should be performed. For the automation of this process for large-scale screening, and to provide an indication of the best strategy for data collection, a metric of crystal variability could be useful. Here, measures of the intrinsic variability within protein crystals are presented and their implications for optimal data-collection strategies are discussed.
authors.affiliation: Department of Physics, University of Oxford, Keble Road, Oxford OX1 3RH, England.
authors.forename: Michael G
authors.initials: MG
authors.lastname: Bowler
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, 6 Rue Jules Horowitz, 38042 Grenoble, France.
authors.forename: Matthew W
authors.initials: MW
authors.lastname: Bowler
mesh_terms: D000818:Animals; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D011506:Proteins / Q000737:chemistry*; D006180:Proton-Translocating ATPases / Q000737:chemistry; D020742:rhoA GTP-Binding Protein / Q000737:chemistry
chemical_list: D011506:Proteins; D006180:Proton-Translocating ATPases; D020742:rhoA GTP-Binding Protein
keywords: automation; macromolecular crystallography; microfocus; sample evaluation