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Accurate hydrogen parameters for the amino acid l ‐leucine
Author(s) -
Binns Jack,
Parsons Simon,
McIntyre Garry J.
Publication year - 2016
Publication title -
acta crystallographica section b
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.604
H-Index - 33
ISSN - 2052-5206
DOI - 10.1107/s2052520616015699
Subject(s) - neutron diffraction , intermolecular force , leucine , crystallography , hydrogen bond , crystal structure , diffraction , amino acid , crystal (programming language) , chemistry , neutron , materials science , molecule , physics , organic chemistry , biochemistry , optics , computer science , programming language , quantum mechanics
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.