title: Accurate hydrogen parameters for the amino acid L-leucine.
abstract: The structure of the primary amino acid L-leucine has been determined for the first time by neutron diffraction. This was made possible by the use of modern neutron Laue diffraction to overcome the previously prohibitive effects of crystal size and quality. The packing of the structure into hydrophobic and hydrophilic layers is explained by the intermolecular interaction energies calculated using the PIXEL method. Variable-temperature data collections confirmed the absence of phase transitions between 120 and 300 K in the single-crystal form.
authors.affiliation: Australian Nuclear Science and Technology Organisation, New Illawarra Road, Lucas Heights NSW 2234, Australia.
authors.forename: Jack
authors.initials: J
authors.lastname: Binns
authors.affiliation: EaStCHEM School of Chemistry and Centre for Science at Extreme Conditions, The University of Edinburgh, The King's Buildings, West Mains Road, Edinburgh EH9 3FJ, Scotland.
authors.forename: Simon
authors.initials: S
authors.lastname: Parsons
authors.affiliation: Australian Nuclear Science and Technology Organisation, New Illawarra Road, Lucas Heights NSW 2234, Australia.
authors.forename: Garry J
authors.initials: GJ
authors.lastname: McIntyre
mesh_terms: D018360:Crystallography, X-Ray; D006859:Hydrogen / Q000737:chemistry*; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007930:Leucine / Q000737:chemistry*; D008958:Models, Molecular; D013696:Temperature
chemical_list: D006859:Hydrogen; D007930:Leucine
keywords: Laue diffraction; amino acids; crystal packing; neutron diffraction