Crystallization and preliminary crystallographic analysis of p40 phox, a regulatory subunit of NADPH oxidase

Kazuya Honbou, Satoru Yuzawa, Nobuo N. Suzuki, Yuko Fujioka, Hideki Sumimoto, Fuyuhiko Inagaki

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1018-1020
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number10
DOIs
Publication statusPublished - Oct 1 2006

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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