Crystallization and characterization of bovine liver glutamate dehydrogenase

Peter E. Peterson; Jonathan Pierce; Thomas J. Smith

doi:10.1006/jsbi.1997.3899

Crystallization and characterization of bovine liver glutamate dehydrogenase

Peter E. Peterson, Jonathan Pierce, Thomas J. Smith

Research output: Contribution to journal › Article › peer-review

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Abstract

Bovine liver glutamate dehydrogenase has been crystallized as an abortive complex with glutamic acid, NADH, and an inhibitor, GTP. Crystals of this complex were grown using the sitting drop vapor diffusion method with PEG 8000 as the precipitant and diffract to better than 2.5 Å resolution. The crystals belong to the space group P2₁ with an entire enzyme hexamer in the crystallographic asymmetric unit. Self-rotation and self-Patterson functions clearly define the orientation and position of this hexameric enzyme.

Original language	English (US)
Pages (from-to)	73-77
Number of pages	5
Journal	Journal of Structural Biology
Volume	120
Issue number	1
DOIs	https://doi.org/10.1006/jsbi.1997.3899
State	Published - Oct 1997
Externally published	Yes

ASJC Scopus subject areas

Structural Biology

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title = "Crystallization and characterization of bovine liver glutamate dehydrogenase",

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author = "Peterson, {Peter E.} and Jonathan Pierce and Smith, {Thomas J.}",

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AU - Pierce, Jonathan

AU - Smith, Thomas J.

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AB - Bovine liver glutamate dehydrogenase has been crystallized as an abortive complex with glutamic acid, NADH, and an inhibitor, GTP. Crystals of this complex were grown using the sitting drop vapor diffusion method with PEG 8000 as the precipitant and diffract to better than 2.5 Å resolution. The crystals belong to the space group P21 with an entire enzyme hexamer in the crystallographic asymmetric unit. Self-rotation and self-Patterson functions clearly define the orientation and position of this hexameric enzyme.

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Crystallization and characterization of bovine liver glutamate dehydrogenase

Abstract

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