Crystallization and preliminary crystallographic studies of human indoleamine 2,3-dioxygenase
Journal Article
·
· Acta Crystallographica. Section F
- 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, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 3 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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