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Reducing radiation damage in macromolecular crystals at synchrotron sources

โœ Scribed by Stern, Edward A. ;Yacoby, Yizhak ;Seidler, Gerald T. ;Nagle, Kenneth P. ;Prange, Micah P. ;Sorini, Adam P. ;Rehr, John J. ;Joachimiak, Andrzej


Publisher
International Union of Crystallography
Year
2009
Tongue
English
Weight
424 KB
Volume
65
Category
Article
ISSN
0907-4449

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โœฆ Synopsis


A new strategy is presented to reduce primary X-ray damage in macromolecular crystallography. The strategy is based on separating the diffracting and damaged regions as much as feasible. The source of the radiation damage to macromolecular crystals is from two primary mechanisms: the direct excitations of electrons by absorption, and inelastic scattering of the X-rays. The first produces photoelectrons with their accompanying Auger electrons from relaxation of the core hole and the second creates Compton electrons. The properties of these two mechanisms and calculations of primary X-ray damage quantify how to modify the spatial distribution of X-rays to reduce the deleterious effects of radiation damage. By focusing the incident X-rays into vertical stripes, it is estimated that the survival (the time during which quality diffraction data can be obtained with a given X-ray flux) of large crystals can be increased by at least a factor of 1.6, while for very small platelet crystals the survival can be increased by up to a factor of 14.


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Reduction of X-ray-induced radiation dam
โœ Meents, A. ;Wagner, A. ;Schneider, R. ;Pradervand, C. ;Pohl, E. ;Schulze-Briese, ๐Ÿ“‚ Article ๐Ÿ“… 2007 ๐Ÿ› International Union of Crystallography ๐ŸŒ English โš– 658 KB

The cryocooling of protein crystals to temperatures of around 100 K drastically reduces X-ray-induced radiation damage. The majority of macromolecular data collection is therefore performed at 100 K, yielding diffraction data of higher resolution and allowing structure determination from much smalle