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Acta Crystallogr B. 2007 Jun;63(Pt 3):505-9. Epub 2007 May 16.

Redetermination, invariom-model and multipole refinement of L-ornithine hydrochloride.

Author information

1
Department of Chemistry, M313, School of Biomedical, Biomolecular and Chemical Sciences, University of Western Australia, Crawley, WA 6009, Australia. birger@cyllene.uwa.edu.au

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.

PMID:
17507764
DOI:
10.1107/S0108768107014838
[Indexed for MEDLINE]

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