title: Feasibility of one-shot-per-crystal structure determination using Laue diffraction.
abstract: Crystal size is an important factor in determining the number of diffraction patterns which may be obtained from a protein crystal before severe radiation damage sets in. As crystal dimensions decrease this number is reduced, eventually falling to one, at which point a complete data set must be assembled using data from multiple crystals. When only a single exposure is to be collected from each crystal, the polychromatic Laue technique may be preferable to monochromatic methods owing to its simultaneous recording of a large number of fully recorded reflections per image. To assess the feasibility of solving structures using single Laue images from multiple crystals, data were collected using a 'pink' beam at the CHESS D1 station from groups of lysozyme crystals with dimensions of the order of 20-30 microm mounted on MicroMesh grids. Single-shot Laue data were used for structure determination by molecular replacement and correct solutions were obtained even when as few as five crystals were used.
authors.affiliation: School of Applied and Engineering Physics, Cornell University, Ithaca, New York, USA.
authors.forename: Sterling
authors.initials: S
authors.lastname: Cornaby
authors.forename: Doletha M E
authors.initials: DM
authors.lastname: Szebenyi
authors.forename: Detlef-M
authors.initials: DM
authors.lastname: Smilgies
authors.forename: David J
authors.initials: DJ
authors.lastname: Schuller
authors.forename: Richard
authors.initials: R
authors.lastname: Gillilan
authors.forename: Quan
authors.initials: Q
authors.lastname: Hao
authors.forename: Donald H
authors.initials: DH
authors.lastname: Bilderback
mesh_terms: D000818:Animals; D002645:Chickens; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods*; D005240:Feasibility Studies; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D009113:Muramidase