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

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  • Published: Apr 6, 2015
  • Author: spectroscopyNOW
  • Channels: X-ray Spectrometry
thumbnail image: Journal Highlight: L-Lysine: Exploiting powder X-ray diffraction to complete the set of crystal structures of the 20 directly encoded proteinogenic amino acids
Modern powder X-ray diffraction methods have been exploited to determine the crystal structure of L-lysine.

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, 2015, 54, 3973-3977
P. Andrew Williams, Colan E. Hughes and Kenneth D. M. Harris

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.

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