Crystallization and preliminary crystallographic studies of human indoleamine 2,3-dioxygenase
- Biometal Science Laboratory, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148 (Japan)
- Department of Biochemistry, Yamagata University School of Medicine, Yamagata 990-9585 (Japan)
Human indoleamine 2,3-dioxygenase, a haem-containing dioxygenase, was crystallized. The crystal diffracted to 2.3 Å resolution. 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{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 86.1, b = 98.0, c = 131.0 Å. Diffraction data were collected to 2.3 Å resolution.
- OSTI ID:
- 22356291
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 3; Other Information: PMCID: PMC2197179; PMID: 16511306; PUBLISHER-ID: fw5067; OAI: oai:pubmedcentral.nih.gov:2197179; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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