Precision neutron diffraction structure determination of protein and nucleic acid components. XVII. Molecular and crystal structure of the amino acid glycine hydrochloride

Autor:	A. R. Al‐Karaghouli, Mogens S. Lehmann, Jacques J. Verbist, F. E. Cole, C. R. Miskell, Thomas F. Koetzle
Rok vydání:	1975
Předmět:	chemistry.chemical_classification Hydrogen Hydrogen bond Neutron diffraction General Physics and Astronomy chemistry.chemical_element Crystal structure Amino acid Bond length Crystallography Molecular geometry chemistry Molecule Physical and Theoretical Chemistry
Zdroj:	The Journal of Chemical Physics. 63:1360-1366
ISSN:	1089-7690 0021-9606
DOI:	10.1063/1.431523
Popis:	The amino acid salt glycine hydrochloride, H3N+⋅CH2⋅COOH⋅Cl−, crystallizes in the space group P21/c, a=7.117(2) A, b=5.234(2) A, c=13.745(3) A, β=97.25(1) °. The crystal structure has been refined from three‐dimensional neutron diffraction data to a final R value based on F2 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.
Databáze:	OpenAIRE
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