Glycyl-L-alanine: a multi-temperature neutron study

Silvia C. Capelli, Hans-Beat Burgi, Sax A. Mason, Dylan Jayatilaka

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)949-952
JournalActa Crystallographica Section C: Structural Chemistry
Publication statusPublished - 2014


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