The structure of L-ornithine hydrochloride, C5H13N2O2+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.
|Journal||Acta Crystallographica. Section B: Structual Science.|
|Publication status||Published - 2007|
Dittrich, B., Munshi, P., & Spackman, M. (2007). Redetermination, invariom-model and multipole refinement of L-ornithine hydrochloride. Acta Crystallographica. Section B: Structual Science., 63(3), 505-509. https://doi.org/10.1107/S0108768107014838