Expression, purification, crystallization and preliminary X-ray diffraction analysis of the soluble domain of PPA0092, a putative nitrite reductase from Propionibacterium acnes.
The soluble domain (residues 483-913) of PPA0092, a putative copper-containing nitrite reductase from Propionibacterium acnes KPA171202, has been overexpressed in Escherichia coli. The purified recombinant protein was crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected and processed to a maximum resolution of 2.4 A. The crystal belonged to space group P2(1)3, with unit-cell parameters a = b = c = 108.63 A. Preliminary diffraction data show that one molecule is present in the asymmetric unit; this corresponds to a V(M) of 2.1 A(3) Da(-1).
Nojiri
Masaki
M
Bioinorganic Chemistry Laboratory, Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
Shirota
Felicia
F
Hira
Daisuke
D
Suzuki
Shinnichiro
S
D000595:Amino Acid Sequence; D000693:Anaerobiosis; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D008969:Molecular Sequence Data; D009566:Nitrates / Q000737:chemistry / Q000378:metabolism; D009572:Nitrite Reductases / Q000096:biosynthesis* / Q000737:chemistry* / Q000235:genetics; D009584:Nitrogen / Q000737:chemistry / Q000378:metabolism; D010101:Oxygen Consumption; D011425:Propionibacterium acnes / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000502:physiology
D001426:Bacterial Proteins; D009566:Nitrates; D009572:Nitrite Reductases; C052695:nitrite reductase, copper-containing; D009584:Nitrogen