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Using neutron protein crystallography to understand enzyme mechanisms.


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.

SUBMITTER: Glusker JP 

PROVIDER: S-EPMC2967424 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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Using neutron protein crystallography to understand enzyme mechanisms.

Glusker Jenny P JP   Carrell H L HL   Kovalevsky Andrey Y AY   Hanson Leif L   Fisher S Zoe SZ   Mustyakimov Marat M   Mason Sax S   Forsyth Trevor T   Langan Paul P  

Acta crystallographica. Section D, Biological crystallography 20101020 Pt 11


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. ...[more]

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