Accurate H-atom parameters for the two polymorphs of L-histi­dine at 5, 105 and 295 K

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dc.contributor.authorNovelli, Gen_AU
dc.contributor.authorMcMonagle, CJen_AU
dc.contributor.authorKleemiss, Fen_AU
dc.contributor.authorProbert, MRen_AU
dc.contributor.authorPuschmann, Hen_AU
dc.contributor.authorGrabowsky, Sen_AU
dc.contributor.authorMaynard-Casely, HEen_AU
dc.contributor.authorMcIntyre, GJen_AU
dc.contributor.authorParsons, Sen_AU
dc.date.accessioned2021-12-16T23:59:04Zen_AU
dc.date.available2021-12-16T23:59:04Zen_AU
dc.date.issued2021-10-01en_AU
dc.date.statistics2021-11-23en_AU
dc.description.abstractThe crystal structure of the monoclinic polymorph of the primary amino acid L-histi­dine has been determined for the first time by single-crystal neutron diffraction, while that of the orthorhombic polymorph has been reinvestigated with an untwinned crystal, improving the experimental precision and accuracy. For each polymorph, neutron diffraction data were collected at 5, 105 and 295 K. Single-crystal X-ray diffraction experiments were also performed at the same temperatures. The two polymorphs, whose crystal packing is interpreted by intermolecular interaction energies calculated using the Pixel method, show differences in the energy and geometry of the hydrogen bond formed along the c direction. Taking advantage of the X-ray diffraction data collected at 5 K, the precision and accuracy of the new Hirshfeld atom refinement method im­ple­mented in NoSpherA2 were probed choosing various settings of the functionals and basis sets, together with the use of explicit clusters of molecules and enhanced rigid-body restraints for H atoms. Equivalent atomic coordinates and aniso­tropic displacement parameters were com­pared and found to agree well with those obtained from the corresponding neutron structural models.© International Union of Crystallographyen_AU
dc.identifier.citationNovelli, G., McMonagle, C. J., Kleemiss, F., Probert, M., Puschmann, H., Grabowsky, S., Maynard-Casely, H. E., McIntyre, G. J., & Parsons, S. (2021). Accurate H-atom parameters for the two polymorphs of L-histi­dine at 5, 105 and 295 K. Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 77(5). 785-800. doi:10.1107/S205252062100740Xen_AU
dc.identifier.issn2052-5206en_AU
dc.identifier.issue5en_AU
dc.identifier.journaltitleActa Crystallographica Section B: Structural Science, Crystal Engineering and Materialsen_AU
dc.identifier.pagination785-800en_AU
dc.identifier.urihttps://doi.org/10.1107/S205252062100740Xen_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/12520en_AU
dc.identifier.volume77en_AU
dc.language.isoenen_AU
dc.publisherInternational Union of Crystallographyen_AU
dc.subjectAmino acidsen_AU
dc.subjectHistidineen_AU
dc.subjectNeutron diffractionen_AU
dc.subjectLaue methoden_AU
dc.subjectCrystal structureen_AU
dc.subjectX-ray diffractionen_AU
dc.titleAccurate H-atom parameters for the two polymorphs of L-histi­dine at 5, 105 and 295 Ken_AU
dc.typeJournal Articleen_AU
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