源自红球菌属菌株RHA1的联苯双加氧酶末端加氧酶组分的结晶。
Crystallization of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1.
作者信息
Nagarajan Venugopalan, Sakurai Nobuyuki, Kubota Miho, Nonaka Takamasa, Nagumo Hiroaki, Takeda Hisashi, Nishizaki Tomoko, Masai Eiji, Fukuda Masao, Mitsui Yukio, Senda Toshiya
机构信息
Division of Protein Engineering, Department of BioEngineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
出版信息
Protein Pept Lett. 2003 Aug;10(4):412-7. doi: 10.2174/0929866033478889.
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.
利用一种新型过表达系统在重组红球菌菌株中使联苯双加氧酶的末端加氧酶组分（BphA1A2复合物）过表达并进行纯化。纯化后的酶已通过悬滴气相扩散法结晶，并进行了X射线衍射分析。晶体属于空间群为P4(1)2(1)2或P4(3)2(1)2的四方晶系，衍射分辨率优于2.2埃。
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