Crystallization and preliminary crystallographic analysis of p40phox, a regulatory subunit of NADPH oxidase.
p40(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(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 A resolution at 100 K using synchrotron radiation. The crystal belongs to space group C222(1), with unit-cell parameters a = 146.27, b = 189.81, c = 79.88 A. This crystal was estimated to contain two or three protein molecules per asymmetric unit from the acceptable range of volume-to-weight ratio values.
Honbou
Kazuya
K
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N-12, W-6, Kita-ku, Sapporo 060-0812, Japan.
Yuzawa
Satoru
S
Suzuki
Nobuo N
NN
Fujioka
Yuko
Y
Sumimoto
Hideki
H
Inagaki
Fuyuhiko
F
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D019255:NADPH Oxidases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D021122:Protein Subunits / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D021122:Protein Subunits; D019255:NADPH Oxidases; C113333:NCF4 protein, human