title: Preliminary structural studies of Escherichia coli isopentenyl diphosphate isomerase.
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.
authors.affiliation: Institut de Recherches Microbiologiques Jean-Marie Wiame, Avenue E. Gryson 1, B-1070 Brussels, Belgium.
authors.forename: Y
authors.initials: Y
authors.lastname: Oudjama
authors.forename: V
authors.initials: V
authors.lastname: Durbecq
authors.forename: G
authors.initials: G
authors.lastname: Sainz
authors.forename: B
authors.initials: B
authors.lastname: Clantin
authors.forename: C
authors.initials: C
authors.lastname: Tricot
authors.forename: V
authors.initials: V
authors.lastname: Stalon
authors.forename: V
authors.initials: V
authors.lastname: Villeret
authors.forename: L
authors.initials: L
authors.lastname: Droogmans
mesh_terms: D019748:Carbon-Carbon Double Bond Isomerases / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D045782:Hemiterpenes; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D045782:Hemiterpenes; D011994:Recombinant Proteins; D019748:Carbon-Carbon Double Bond Isomerases; C021453:isopentenyldiphosphate delta-isomerase