Abstract
To bridge the gap between traditional multilayer and crystal optics a high-resolution multilayer monochromator with a bandwidth of 0.22% has been designed and installed on a bending-magnet beamline (F3) at the Cornell High Energy Synchrotron Source (CHESS) to provide an unfocused monochromatic X-ray beam for protein crystallography experiments. Crystallographic data of excellent quality from a medium-sized protein, Concanavalin A, were collected and processed using standard Crystallographic programs. The data were successfully used for a structure solution and refinement. The flux from the multilayer monochromator is enhanced, relative to that from a flat Si(111) monochromator, by a factor of 5; consequently, data collection is faster and/or smaller samples may be used. At the same time, the bandwidth is narrow enough to avoid streaked spots. This experiment suggests that multilayer optics may play a valuable role in satisfying the demands of the structural biology community for rapid X-ray data collection, particularly at under-utilized bending-magnet beamlines. © 2005 International Union of Crystallography Printed in Great Britain - all rights reserved.
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Englich, U., Kazimirov, A., Shen, Q., Bilderback, D. H., Gruner, S. M., & Hao, Q. (2005). Crystallographic data collection using a 0.22% bandwidth multilayer. Journal of Synchrotron Radiation, 12(3), 345–348. https://doi.org/10.1107/S0909049505002645
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