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Cloning, expression, purification and preliminary crystallographic characterization of a shikimate dehydrogenase from Corynebacterium glutamicum

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The shikimate dehydrogenase from Corynebacterium glutamicum has been cloned into an Escherichia coli expression vector, overexpressed and purified. Native crystals were obtained by the vapour‐diffusion technique using 2‐methyl‐2,4‐pentanediol as a precipitant. The crystals belong to the centred monoclinic space group C2, with unit‐cell parameters a = 118.77, b = 63.17, c = 35.67 Å, β = 92.26° (at 100 K), and diffract to 1.64 Å on a synchrotron X‐ray source. The asymmetric unit is likely to contain one molecule, corresponding to a packing density of 2.08 Å3 Da−1 and a solvent content of about 41%.
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Keywords: Corynebacterium glutamicum; shikimate dehydrogenase

Document Type: Research Article

Affiliations: Institute for Biochemistry, University of Köln, Zülpicher Strasse 47, Köln, NRW 50974, Germany

Publication date: July 1, 2006

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