Complementarity of Neutron and Ultrahigh Resolution Synchrotron X-ray Protein Crystallography Studies: Results with Concanavalin A at Cryo and Room Temperature
J.R. Helliwell , H.J. Price, A. Deacon , J. Raftery and J. Habash
Department of Chemistry, University of Manchester, M13 9PL, UK
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The complementarity of synchrotron derived ultrahigh resolution X-ray and neutron protein crystallography is explored via an ensemble of plant lectin concanavalin A crystal structures. Thus a resume of a study of a cryo 0.94 A and a neutron (+X-ray) protein crystal 2.4 A structure at room temperature is made and these are then compared in their efficiency to determine the positions of the bound solvent atoms i.e. as hydrogens or deuteriums. First results are also presented of comparisons of two ultrahigh resolution protein crystal structures, the 0.94 A and a new 0.92 A structure. Thus the variability of the two cryo structures, at very fine detail, is described; this variability is in the multiple occupancies of side chains. Overall, one can see that a "complete" structure definition, with today's experimental capabilities, is possible and can include structure ensemble variations.
DOI: 10.12693/APhysPolA.101.583
PACS numbers: 87.64.-t, 87.15.-v, 61.12.-q