Crystallization and preliminary crystallographic studies of human indoleamine 2,3-dioxygenase.
Indoleamine 2,3-dioxygenase (IDO) is a haem-containing dioxygenase that catalyzes the oxidative cleavage of the pyrrole ring of indoleamines by the insertion of molecular oxygen. This reaction is the first and the rate-limiting step in the kynurenine pathway, the major Trp catabolic pathway in mammals. Recombinant human IDO was crystallized by the vapour-diffusion technique. The addition of 4-phenylimidazole as a haem ligand was essential for crystallization. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 86.1, b = 98.0, c = 131.0 A. Diffraction data were collected to 2.3 A resolution.
Oda
Shun-ichiro
S
Biometal Science Laboratory, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Sugimoto
Hiroshi
H
Yoshida
Tadashi
T
Shiro
Yoshitsugu
Y
D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D006801:Humans; D007093:Imidazoles / Q000737:chemistry; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D007093:Imidazoles; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D011994:Recombinant Proteins; C033023:4(5)-phenylimidazole