PMID:11468415
| Citation |
Kemp, LE, Bond, CS and Hunter, WN (2001) Crystallization and preliminary X-ray diffraction studies of recombinant Escherichia coli 4-diphosphocytidyl-2-C-methyl-D-erythritol synthetase. Acta Crystallogr. D Biol. Crystallogr. 57:1189-91 |
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| 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. |
| Links | |
| Keywords |
Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Nucleotidyltransferases/biosynthesis; Nucleotidyltransferases/chemistry; Nucleotidyltransferases/genetics; Protein Conformation; Recombinant Proteins/chemistry |
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