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.Full text not available from this repository.
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.
|School or Research Centre:||Birkbeck Schools and Research Centres > School of Science > Biological Sciences|
|Date Deposited:||23 Jun 2011 08:13|
|Last Modified:||17 Apr 2013 12:20|
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