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L-lysine: Exploiting powder X-ray diffraction to complete the set of crystal structures of the 20 directly encoded proteinogenic amino acids

Williams, P. Andrew, Hughes, Colan Evan and Harris, Kenneth David Maclean 2015. L-lysine: Exploiting powder X-ray diffraction to complete the set of crystal structures of the 20 directly encoded proteinogenic amino acids. Angewandte Chemie - International Edition 54 (13) , pp. 3973-3977. 10.1002/anie.201411520

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Abstract

During the last 75 years, crystal structures have been reported for 19 of the 20 directly encoded proteinogenic amino acids in their natural (enantiomerically pure) form. The crystal structure is now reported for the final member of this set: L-lysine. As crystalline L-lysine has a strong propensity to incorporate water under ambient atmospheric conditions to form a hydrate phase, the pure (non-hydrate) crystalline phase can be obtained only by dehydration under rigorously anhydrous conditions, resulting in a microcrystalline powder sample. For this reason, modern powder X-ray diffraction methods have been exploited to determine the crystal structure in this final, elusive case.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Advanced Research Computing @ Cardiff (ARCCA)
Chemistry
Subjects: Q Science > QD Chemistry
Publisher: Wiley-Blackwell
ISSN: 1433-7851
Last Modified: 04 Jun 2017 07:59
URI: http://orca.cf.ac.uk/id/eprint/71236

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