title: Glycyl-L-alanine: a multi-temperature neutron study.
abstract: Neutron diffraction data have been collected at 12, 50, 150 and 295 K for the dipeptide glycyl-L-alanine, C5H10N2O3, in order to obtain accurate positional and anisotropic displacement parameters for the H atoms. The values of these parameters serve as a benchmark for assessing the equivalent parameters obtained from a so-called Hirshfeld-atom refinement of X-ray diffraction data described elsewhere [Capelli et al. (2014). IUCrJ, 1, 361-379]. The flexibility of the glycyl-L-alanine molecule in the solid and the hydrogen-bonding interactions as a function of temperature are also considered.
authors.affiliation: Dipartimento di Chimica, Universitá degli Studi di Milano, Via Golgi 19, 20133 Milano, Italy.
authors.forename: Silvia C
authors.initials: SC
authors.lastname: Capelli
authors.affiliation: Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
authors.forename: Hans-Beat
authors.initials: HB
authors.lastname: Bürgi
authors.affiliation: Intitut Laue-Langevin, 71 Avenue des Martyrs, 38000 Grenoble, France.
authors.forename: Sax A
authors.initials: SA
authors.lastname: Mason
authors.affiliation: School of Chemistry and Biochemistry, The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia.
authors.forename: Dylan
authors.initials: D
authors.lastname: Jayatilaka
mesh_terms: D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000737:chemistry*; D009502:Neutrons; D013696:Temperature; D014961:X-Ray Diffraction
chemical_list: D004151:Dipeptides; C007873:glycyl-beta-alanine
keywords: crystal structure; dipeptide; glycyl-l-alanine; multi-temperature study; neutron diffraction