Preliminary structural studies of Escherichia coli isopentenyl diphosphate isomerase.
Acta crystallographica. Section D, Biological crystallography(2001)
摘要
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.
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关键词
escherichia coli
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