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Glusker JP , Carrell HL , Kovalevsky AY , Hanson L , Fisher SZ , Mustyakimov M , Mason S , Forsyth T , Langan P
Using neutron protein crystallography to understand enzyme mechanisms
Acta Crystallogr D Biol Crystallogr. 2010 Nov;66(Pt 11) :1257-61
PMID: 21041947   
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Abstract
A description is given of the results of neutron diffraction studies of the structures of four different metal-ion complexes of deuterated D-xylose isomerase. These represent four stages in the progression of the biochemical catalytic action of this enzyme. Analyses of the structural changes observed between the various three-dimensional structures lead to some insight into the mechanism of action of this enzyme.
Notes
Glusker, Jenny P Carrell, H L Kovalevsky, Andrey Y Hanson, Leif Fisher, S Zoe Mustyakimov, Marat Mason, Sax Forsyth, Trevor Langan, Paul England Acta crystallographica. Section D, Biological crystallography Acta Crystallogr D Biol Crystallogr. 2010 Nov;66(Pt 11):1257-61. Epub 2010 Oct 20.