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Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase by Makie A. Taal; Svetlana E. Sedelnikova; Sergey N. Ruzheinikov; Patrick J. Baker; David W. Rice is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase about?

Glutamate racemase (MurI, RacE; E.C.5.1.1.3) catalyses the cofactorindependent conversion of l-glutamate to d-glutamate, an essential step in the synthesis of components of the bacterial cell wall. The gene for RacE from Bacillus subtilis has been cloned and the protein expressed in Escherichia coli, puri®ed and crystallized in the presence of l-glutamate using the hanging-drop method of vapour diffusion with diammonium tartrate as the precipitant. The crystals belong to the monoclinic space group C2, with approximate unit-cell parameters a = 133.6, b = 60.1, c = 126.2 A Ê , = 117.6 . Consideration of the possible values of V M suggests that the asymmetric unit contains either two (V M = 3.75 A Ê 3 Da À1 ) or three (V M = 2.5 A Ê 3 Da À1 ) subunits. The crystals diffract X-rays to at least 2.1 A Ê resolution on a synchrotron-radiation source and are suitable for structural studies. Determination of the structure may provide insight into the molecular basis of substrate recognition and catalysis by this enzyme.

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Author

Makie A. Taal; Svetlana E. Sedelnikova; Sergey N. Ruzheinikov; Patrick J. Baker; David W. Rice

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)