Accurate hydrogen parameters for the amino acid Lleucine.

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 singlecrystal form. [ABSTRACT FROM AUTHOR]