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The neutron structure of the formyl peptide receptor antagonist Cyclosporin H (CsH) unambiguously determines the solvent and Hydrogen-bonding structure for crystal form II

Gardberg, A.S. and Potter, B.S. and Palmer, Rex A. and McIntyre, G.J. and Myles, D.A.A. (2011) The neutron structure of the formyl peptide receptor antagonist Cyclosporin H (CsH) unambiguously determines the solvent and Hydrogen-bonding structure for crystal form II. Journal of Chemical Crystallography 41 (4), pp. 470-480. ISSN 1074-1542.

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Official URL: http://dx.doi.org/10.1007/s10870-010-9903-7

Abstract

Single-crystal neutron diffraction data were collected at 20 K to a resolution of 1.05 on a crystal of the inverse formyl peptide receptor agonist cyclosporin H, CsH, (crystal form II, CsH-II) on the Laue diffractometer VIVALDI at the Institut Laue-Langevin (Grenoble). The solvent structure and hydrogen bonding network of CsH-II have been unambiguously determined by single-crystal neutron diffraction; the agreement factor R(F (2)) is 13.5% for all 2726 reflections. All hydrogen atom positions, including methyl-group orientations, have been determined by crystallographic refinement. The neutron structure of cyclosporin provides unique and complementary insights into methyl orientation, hydrogen-bonding, and solvent interactions that are not available from X-ray analysis alone.

Item Type: Article
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 23 Jun 2011 08:13
Last Modified: 17 Apr 2013 12:20
URI: http://eprints.bbk.ac.uk/id/eprint/3632

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