Escherichia coli isopentenyl diphosphate isomerase, an enzyme catalyzing a
key step in isoprenoid biosynthesis, has been produced in selenomethionyl f
orm. The protein was purified and crystallized by the hanging-drop vapour-d
iffusion method. Crystals display trigonal symmetry, with unit-cell paramet
ers a = b = 71.3, c = 61.7 Angstrom, and diffract to 1.45 Angstrom resoluti
on.