Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductase.
Biliverdin reductase (BVR) catalyzes the final step of haem degradation and converts biliverdin to bilirubin using NAD(P)H as an electron donor. This paper deals with the first crystallization and preliminary crystallographic study of recombinant rat BVR expressed in Escherichia coli. Crystals of BVR were obtained by the sitting-drop vapour-diffusion method. Using synchrotron radiation at station BL44B2 of SPring-8, Japan, BVR diffraction data were collected to 1.6 A resolution. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 58.89, b = 70.41, c = 87.76 A. The complete determination of the crystallographic structure is currently in progress using MAD (multiwavelength anomalous diffraction) data from an Ir-derivative crystal.
Sun
D
D
Department of Biochemistry, Yamagata University School of Medicine, Yamagata 990-9585, Japan.
Sato
M
M
Yoshida
T
T
Shimizu
H
H
Miyatake
H
H
Adachi
S
S
Shiro
Y
Y
Kikuchi
A
A
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D010088:Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D044925:Oxidoreductases Acting on CH-CH Group Donors; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
D011994:Recombinant Proteins; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C019789:biliverdin reductase