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

Angew Chem Int Ed Engl. 2015 Mar 23;54(13):3973-7. doi: 10.1002/anie.201411520. Epub 2015 Feb 4.

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.

Keywords: L-lysine; amino acids; powder x-ray diffraction; structure determination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Amino Acids / chemistry*
  • Crystallization
  • Hydrogen Bonding
  • Lysine / chemistry*
  • Models, Molecular
  • Molecular Conformation
  • Powders
  • Structure-Activity Relationship
  • X-Ray Diffraction

Substances

  • Amino Acids
  • Powders
  • Lysine