Published September 30, 2006 | Version v1
Journal article

Crystallization and preliminary crystallographic analysis of p40phox, a regulatory subunit of NADPH oxidase

  • 1. Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N-12, W-6, Kita-ku, Sapporo 060-0812 (Japan)
  • 2. CREST, Japan Science and Technology Corporation (Japan)
  • 3. Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8512 (Japan)

Description

Human p40phox was expressed, purified and crystallized. Diffraction data were collected to a resolution of 3.0 Å. p40phox is a cytosolic component of the phagocyte NADPH oxidase, which is responsible for production of the superoxide that kills invasive microorganisms. Full-length p40phox 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 C2221, 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

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309106036256; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225170

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
62
Journal Issue
Pt 10
Journal Page Range
p. 1018-1020
ISSN
1744-3091
CODEN
ACSFCL

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2006
Notes
PMCID: PMC2225170; PMID: 17012801; PUBLISHER-ID: bo5005; OAI: oai:pubmedcentral.nih.gov:2225170