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, 57 (Pt 8), 1189-91

Crystallization and Preliminary X-ray Diffraction Studies of Recombinant Escherichia Coli 4-diphosphocytidyl-2-C-methyl-D-erythritol Synthetase

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Crystallization and Preliminary X-ray Diffraction Studies of Recombinant Escherichia Coli 4-diphosphocytidyl-2-C-methyl-D-erythritol Synthetase

L E Kemp et al. Acta Crystallogr D Biol Crystallogr.

Abstract

Diphosphocytidyl-methylerythritol (DPCME) synthetase is involved in the mevalonate-independent pathway of isoprenoid biosynthesis, where it catalyses the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate and CTP. The Escherichia coli enzyme has been cloned, expressed in high yield, purified and crystallized. Elongated tetragonal prismatic crystals grown by the hanging-drop vapour-diffusion method using polyethylene glycol (PEG) 4000 as the precipitant belong to space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 73.60, c = 175.56 A. Diffraction data have been recorded to 2.4 A resolution using synchrotron radiation.

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