Feasibility of one-shot-per-crystal structure determination using Laue diffraction.
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.
Cornaby
Sterling
S
School of Applied and Engineering Physics, Cornell University, Ithaca, New York, USA.
Szebenyi
Doletha M E
DM
Smilgies
Detlef-M
DM
Schuller
David J
DJ
Gillilan
Richard
R
Hao
Quan
Q
Bilderback
Donald H
DH
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
D009113:Muramidase