Anisotropic displacement parameters of non-hydrogen atoms in proteins from neutron diffraction data measured at multiple temperatures.
Neutron diffraction studies on proteins have so far primarily been used to locate hydrogen (or D) atoms. Structures are usually not refined to high resolution and there has been no emphasis on atomic displacement parameters (ADPs). The function of proteins is linked to their dynamical behavior, which in principle could emerge from an analysis of anisotropic ADPs. A previous X-ray study to obtain anisotropic ADPs by refinement of high resolution X-ray diffraction data from P1 hen egg-white lysozyme (HEWL) at four low temperatures, demonstrated the need for an independent estimate of anisotropic ADPs by neutron diffraction. The aim of this proposal is to obtain anisotropic ADPs by refinement of high resolution neutron data measured at 295K, 180K and 100K in order to address the following questions: i) Can neutron diffraction data provide anisotropic ADPs for proteins? ii) Can the ADPs be related to protein dynamics? iii) Are the ADPs comparable to those obtained from high resolution X-ray studies? Resubmitted as the crystallization conditions used during our previous work unexpectedly needed further optimization. This is now under control as demonstrated in the scientific case.
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Sine Larsen; FORSYTH Victor Trevor; LANGKILDE Annette Eva; MASON, Sax A. and MOSSOU Estelle. (2016). Anisotropic displacement parameters of non-hydrogen atoms in proteins from neutron diffraction data measured at multiple temperatures.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-01-475
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