作者: J.R. Helliwell , H.J. Price , A. Deacon , J. Raftery , J. Habash
DOI: 10.12693/APHYSPOLA.101.583
关键词: Concanavalin A 、 Side chain 、 X-ray crystallography 、 X-ray 、 Protein crystallization 、 Materials science 、 Crystal structure 、 Synchrotron 、 Nuclear magnetic resonance 、 Neutron 、 Crystallography
摘要: The complementarity of synchrotron derived ultrahigh resolution X-ray and neutron protein crystallography is explored via an ensemble plant lectin concanavalin A crystal structures. Thus a resume study cryo 0.94 (+X-ray) 2.4 structure at room temperature made these are then compared in their efficiency to determine the positions bound solvent atoms i.e. as hydrogens or deuteriums. First results also presented comparisons two structures, new 0.92 structure. variability very fine detail, described; this multiple occupancies side chains. Overall, one can see that "complete" definition, with today's experimental capabilities, possible include variations.