PMID:11173482
| Citation |
Oudjama, Y, Durbecq, V, Sainz, G, Clantin, B, Tricot, C, Stalon, V, Villeret, V and Droogmans, L (2001) Preliminary structural studies of Escherichia coli isopentenyl diphosphate isomerase. Acta Crystallogr. D Biol. Crystallogr. 57:287-8 |
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| Abstract |
Escherichia coli isopentenyl diphosphate isomerase, an enzyme catalyzing a key step in isoprenoid biosynthesis, has been produced in selenomethionyl form. The protein was purified and crystallized by the hanging-drop vapour-diffusion method. Crystals display trigonal symmetry, with unit-cell parameters a = b = 71.3, c = 61.7 A, and diffract to 1.45 A resolution. |
| Links | |
| Keywords |
Carbon-Carbon Double Bond Isomerases/chemistry; Carbon-Carbon Double Bond Isomerases/isolation & purification; Cloning, Molecular; Crystallization; Escherichia coli/enzymology; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; X-Ray Diffraction |
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