title: Crystallization and preliminary X-ray diffraction analysis of a complex between the electron-transfer partners hexameric Cu-containing nitrite reductase and pseudoazurin.
abstract: The complex between Cu-containing nitrite reductase (HdNIR) and its electron-donor protein pseudoazurin (HdPAz) from Hyphomicrobium denitrificans has been crystallized. The crystals were obtained from a mixture of the two proteins using the hanging-drop vapour-diffusion method in the presence of polyethylene glycol (PEG) and 2-methyl-2,4-pentanediol (MPD) as precipitants. SDS-PAGE analysis demonstrated that the crystals contained both proteins. The X-ray diffraction experiment was carried out at SPring-8 and diffraction data were collected to 3.3 A resolution. The crystals were tetragonal (space group P4(1)2(1)2), with unit-cell parameters a = b = 130.39, c = 505.55 A. Preliminary analysis indicated that there was one HdNIR and at least two HdPAz molecules in the asymmetric unit of the crystal.
authors.affiliation: Bioinorganic Chemistry Laboratory, Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Hira
authors.forename: Masaki
authors.initials: M
authors.lastname: Nojiri
authors.forename: Shinnichiro
authors.initials: S
authors.lastname: Suzuki
mesh_terms: D042481:Alcaligenes faecalis / Q000201:enzymology; D001400:Azurin / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D003460:Crystallization; D004579:Electron Transport / Q000502:physiology; D020582:Hyphomicrobium / Q000201:enzymology*; D009572:Nitrite Reductases / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D001426:Bacterial Proteins; C047163:pseudoazurin; D001400:Azurin; D009572:Nitrite Reductases; C052695:nitrite reductase, copper-containing