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  • Title: Feasibility of one-shot-per-crystal structure determination using Laue diffraction.
    Author: Cornaby S, Szebenyi DM, Smilgies DM, Schuller DJ, Gillilan R, Hao Q, Bilderback DH.
    Journal: Acta Crystallogr D Biol Crystallogr; 2010 Jan; 66(Pt 1):2-11. PubMed ID: 20057043.
    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.
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