Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme.
The water-soluble portion of rat heme oxygenase-1 which lacks 22 hydrophobic amino-acid residues at the C-terminus was expressed in E. coli and crystallized in the form of a complex with heme by the vapor-diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P41212 or P43212, with unit-cell dimensions of a = b = 56.7, c = 186. 7 A. The crystal contains one heme-heme oxygenase-1 complex in an asymmetric unit and diffracts X-rays beyond 3.0 A resolution with a conventional X-ray source.
Omata
Y
Y
Department of Medical Biochemistry, Kurume University School of Medicine, 67 Asahi-machi, Kurume 830-0011, Japan.
Asada
S
S
Sakamoto
H
H
Fukuyama
K
K
Noguchi
M
M
D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D006418:Heme / Q000737:chemistry* / Q000378:metabolism; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D051547:Heme Oxygenase-1; D046911:Macromolecular Substances; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D046911:Macromolecular Substances; D011993:Recombinant Fusion Proteins; D006418:Heme; D006419:Heme Oxygenase (Decyclizing); D051547:Heme Oxygenase-1