Preliminary structural studies of Escherichia coli isopentenyl diphosphate isomerase.
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.
Oudjama
Y
Y
Institut de Recherches Microbiologiques Jean-Marie Wiame, Avenue E. Gryson 1, B-1070 Brussels, Belgium.
Durbecq
V
V
Sainz
G
G
Clantin
B
B
Tricot
C
C
Stalon
V
V
Villeret
V
V
Droogmans
L
L
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
D045782:Hemiterpenes; D011994:Recombinant Proteins; D019748:Carbon-Carbon Double Bond Isomerases; C021453:isopentenyldiphosphate delta-isomerase