Crystallization and preliminary crystallographic analysis of p40{sup phox}, a regulatory subunit of NADPH oxidase
- Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N-12, W-6, Kita-ku, Sapporo 060-0812 (Japan)
- Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8512 (Japan)
Human p40{sup phox} was expressed, purified and crystallized. Diffraction data were collected to a resolution of 3.0 Å. p40{sup phox} is a cytosolic component of the phagocyte NADPH oxidase, which is responsible for production of the superoxide that kills invasive microorganisms. Full-length p40{sup phox} was expressed in Escherichia coli, purified and crystallized by the sitting-drop vapour-diffusion method at 293 K using polyethylene glycol 20 000 as a precipitant. Diffraction data were collected to 3.0 Å resolution at 100 K using synchrotron radiation. The crystal belongs to space group C222{sub 1}, with unit-cell parameters a = 146.27, b = 189.81, c = 79.88 Å. This crystal was estimated to contain two or three protein molecules per asymmetric unit from the acceptable range of volume-to-weight ratio values.
- OSTI ID:
- 22356353
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 10; Other Information: PMCID: PMC2225170; PMID: 17012801; PUBLISHER-ID: bo5005; OAI: oai:pubmedcentral.nih.gov:2225170; 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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