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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
Author(s) -
Williams P. Andrew,
Hughes Colan E.,
Harris Kenneth D. M.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201411520
Subject(s) - anhydrous , microcrystalline , hydrate , powder diffraction , crystallography , lysine , crystal structure , amino acid , crystal (programming language) , chemistry , dehydration , phase (matter) , diffraction , materials science , organic chemistry , physics , biochemistry , optics , computer science , programming language
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.