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

Acta Crystallogr Sect F Struct Biol Cryst Commun

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

Published: July 2006

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 angstroms, beta = 92.26 degrees (at 100 K), and diffract to 1.64 angstroms on a synchrotron X-ray source. The asymmetric unit is likely to contain one molecule, corresponding to a packing density of 2.08 angstroms3 Da(-1) and a solvent content of about 41%.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242951PMC
http://dx.doi.org/10.1107/S1744309106017805DOI Listing

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