A neutron diffraction study ofa-glycylglycine, C4HsN203, has been carried out at 82 K.

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A neutron diffraction study of the amino acid salt L-phenylalanine.HC1 (C9HI2NO+CI -) has been carried out. Space group P2t2121; a=27.763 (17), b=7.059 (4), c= 5.380 (5)

Precision neutron diffraction structure determination of protein and nucleic acid components. XV. Crystal and molecular structure of the amino acid Lvaline hydrochloride J. Chem. Phys. 60, 4690 (1974); 10.1063/1.1680969 Precision neutron diffraction structure determination of protein and nucleic acid components. XII. A study of hydrogen bonding in the purinepyrimidine base pair 9methyladenine · 1methylthymine J. Chem. Phys. 59, 915 (1973); 10.1063/1.1680114 Precision neutron diffraction structure determination of protein and nucleic acid components. X. A comparison between the crystal and molecular structures of Ltyrosine and Ltyrosine hydrochloride The amino acid salt glycine hydrochloride, H 3 N'·CH,·COOH·CI-, crystallizes in the space group P2 j /c, a = 7.117(2) A, b = 5.234(2) A, C = 13.745(3) A, (3 = 97.25 (1),. The crystal structure has been refined from three-dimensional neutron diffraction data to a final R value based on F' of 0.058. Estimated standard deviations in bond distances and angles are approximately 0.002 A and 0.2°, respectively. There is a network of hydrogen bonds with the chloride ions linking three neighboring glycines to form layers parallel to the ab plane. One ammonium group hydrogen is involved in two weak electrostatic interactions; these interactions join the single layers to form parallel double layers but are probably too weak to be termed hydrogen bonds.

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