Accurate hydrogen parameters for the amino acid L-leucine
No Thumbnail Available
Date
2016-01
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
International Union of Crystallography
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. © International Union of Crystallography
Description
Keywords
Amino acids, Neutron diffraction, Laue method, Crystal structure, Hydrophylic polymers, Phase transformations, Monocrystals
Citation
Binns, J., Parsons, S. & McIntyre, G. J. (2016). Accurate hydrogen parameters for the amino acid L-leucine. Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 72(6), 885-892. doi:10.1107/S2052520616015699