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