title: L-Lysine: exploiting powder X-ray diffraction to complete the set of crystal structures of the 20 directly encoded proteinogenic amino acids.
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.
authors: School of Chemistry, Cardiff University, Cardiff CF10 3AT, Wales (UK).
authors: P Andrew
authors: PA
authors: Williams
authors: Colan E
authors: CE
authors: Hughes
authors: Kenneth D M
authors: KD
authors: Harris
mesh_terms: D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry*; D003460:Crystallization; D006860:Hydrogen Bonding; D008239:Lysine / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D011208:Powders; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
chemical_list: D000596:Amino Acids; D011208:Powders; D008239:Lysine
keywords: L-lysine; amino acids; powder x-ray diffraction; structure determination