Open AccessCrystallization and preliminary crystallographic studies of human indoleamine 2,3‐dioxygenase
Author(s) -
Oda Shunichiro,
Sugimoto Hiroshi,
Yoshida Tadashi,
Shiro Yoshitsugu
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106003356
Subject(s) - indoleamine 2,3 dioxygenase , crystallization , chemistry , kynurenine , dioxygenase , pyrrole , crystallography , stereochemistry , kynurenine pathway , tryptophan , biochemistry , enzyme , organic chemistry , amino acid
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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 86.1, b = 98.0, c = 131.0 Å. Diffraction data were collected to 2.3 Å resolution.