Crystallization and preliminary crystallographic analysis of the autoinhibited form of the tandem SH3 domain of p47phox

Satoru Yuzawa, Nobuo N. Suzuki, Yuko Fujioka, Kenji Ogura, Hideki Sumimoto, Fuyuhiko Inagaki

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Abstract

p47phox is a cytosolic component of the phagocyte NADPH oxidase, which is responsible for the production of the superoxide which kills invasive microorgamisms. A recombinant form of a histidine-tagged tandem SH3 domain of the p47phox-containing polybasic autoinhibited region was expressed in Escherichia coli and purified and crystallized by the sitting-drop vapour-diffusion method at 293 K using polyethylene glycol 6000 as a precipitant. Diffraction data were collected to 2.15 Å resolution at 100 K using synchrotron radiation. The crystal belongs to space group P4 1212 or P43212, with unit-cell parameters a = 100.02, c = 44.94 Å. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (VM) of 2.6 Å3 Da-1 and a solvent content of 52% by volume.

Original languageEnglish
Pages (from-to)1479-1480
Number of pages2
JournalActa Crystallographica - Section D Biological Crystallography
Volume59
Issue number8
DOIs
Publication statusPublished - Aug 1 2003

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All Science Journal Classification (ASJC) codes

  • Structural Biology

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