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Preliminary structural studies of Escherichia coli isopentenyl diphosphate isomerase
Y Oudjama1, V Durbecq, G Sainz
1Institut de Recherches Microbiologiques Jean-Marie Wiame, Avenue E. Gryson 1, B-1070 Brussels, Belgium.
Acta Crystallographica. Section D, Biological Crystallography
|February 15, 2001
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.