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Publication Abstract from PubMed

Crystal structure determinations of biological macromolecules are limited by the availability of sufficiently sized crystals and by the fact that crystal quality deteriorates during data collection owing to radiation damage. Exploiting a micrometre-sized X-ray beam, high-precision diffractometry and shutterless data acquisition with a pixel-array detector, a strategy for collecting data from many micrometre-sized crystals presented to an X-ray beam in a vitrified suspension is demonstrated. By combining diffraction data from 80 Trypanosoma brucei procathepsin B crystals with an average volume of 9 microm(3), a complete data set to 3.0 A resolution has been assembled. The data allowed the refinement of a structural model that is consistent with that previously obtained using free-electron laser radiation, providing mutual validation. Further improvements of the serial synchrotron crystallography technique and its combination with serial femtosecond crystallography are discussed that may allow the determination of high-resolution structures of micrometre-sized crystals.

Serial crystallography on in vivo grown microcrystals using synchrotron radiation.,Gati C, Bourenkov G, Klinge M, Rehders D, Stellato F, Oberthur D, Yefanov O, Sommer BP, Mogk S, Duszenko M, Betzel C, Schneider TR, Chapman HN, Redecke L IUCrJ. 2014 Feb 10;1(Pt 2):87-94. doi: 10.1107/S2052252513033939. eCollection, 2014 Mar 1. PMID:25075324^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.