Crystallization of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1.
The terminal oxygenase component of the biphenyl dioxygenase (BphA1A2 complex) was over-expressed with a novel over expression system in recombinant Rhodococcus strain and purified. The purified enzyme has been crystallized by the hanging drop vapor diffusion method and subjected to X-ray diffraction analysis. The crystals belong to the tetragonal system in the space group P4(1)2(1)2 or P4(3)2(1)2 and diffract to better than 2.2A resolution.
Nagarajan
Venugopalan
V
Division of Protein Engineering, Department of BioEngineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Sakurai
Nobuyuki
N
Kubota
Miho
M
Nonaka
Takamasa
T
Nagumo
Hiroaki
H
Takeda
Hisashi
H
Nishizaki
Tomoko
T
Masai
Eiji
E
Fukuda
Masao
M
Mitsui
Yukio
Y
Senda
Toshiya
T
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D003627:Data Interpretation, Statistical; D015971:Gene Expression Regulation, Enzymologic; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D010105:Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012240:Rhodococcus / Q000201:enzymology* / Q000235:genetics
D007506:Iron-Sulfur Proteins; D011994:Recombinant Proteins; D010105:Oxygenases; C074161:biphenyl-2,3-dioxygenase