Crystallization and preliminary X-ray characterization of rat liver acyl-CoA oxidase.
A recombinant form of the flavoenzyme acyl-CoA oxidase from rat liver has been crystallized by the hanging-drop vapour-diffusion technique using PEG 20 000 as a precipitating agent. The crystals grew as yellow prisms, with unit-cell parameters a = 71.05, b = 87.29, c = 213.05 A, alpha = beta = gamma = 90 degrees. The crystals exhibit the symmetry of space group P2(1)2(1)2(1) and are most likely to contain a dimer in the asymmetric unit, with a V(M) value of 2.21 A(3) Da(-1). The crystals diffract to a resolution of 2.5 A at beamline BL6A of the Photon Factory. Two heavy-atom derivatives have been identified.
Nakajima
Y
Y
Department of Chemistry, Graduate School of Science, Osaka City University, Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan.
Miyahara
I
I
Hirotsu
K
K
Nishina
Y
Y
Shiga
K
K
Setoyama
C
C
Tamaoki
H
H
Miura
R
R
D042962:Acyl-CoA Oxidase; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008099:Liver / Q000201:enzymology*; D010088:Oxidoreductases / Q000737:chemistry*; D011487:Protein Conformation; D051381:Rats
D010088:Oxidoreductases; D042962:Acyl-CoA Oxidase