title: Redetermination, invariom-model and multipole refinement of L-ornithine hydrochloride.
abstract: The structure of L-ornithine hydrochloride, C(5)H(13)N(2)O2+Cl(-), has been redetermined at 100 K by single-crystal X-ray diffraction within a project that aims to generate accurate bond-distance restraints for the invariom refinement of proteins. The high-resolution data were subject to an invariom and a multipole refinement, and the resulting electron densities on a grid were compared. Improvements in the conventional R factor obtained by multipole modelling were smaller than in other structures containing solely the elements CHNO owing to Cl core scattering. Cruickshank's diffraction-component precision index and Stevens & Coppens suitability factor are discussed.
authors.affiliation: Department of Chemistry, M313, School of Biomedical, Biomolecular and Chemical Sciences, University of Western Australia, Crawley, WA 6009, Australia. birger@cyllene.uwa.edu.au
authors.forename: B
authors.initials: B
authors.lastname: Dittrich
authors.forename: P
authors.initials: P
authors.lastname: Munshi
authors.forename: M A
authors.initials: MA
authors.lastname: Spackman
mesh_terms: D018360:Crystallography, X-Ray; D008956:Models, Chemical; D015394:Molecular Structure; D009952:Ornithine / Q000737:chemistry*; D055672:Static Electricity; D013237:Stereoisomerism
chemical_list: D009952:Ornithine