Zhou Ruimin, Huang Cong, Zhang Aili, Bell Stephen G, Zhou Weihong, Wong Luet-Lok
Tianjin Key Laboratory of Protein Science, College of Life Sciences, Nankai University, Tianjin, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):964-7. doi: 10.1107/S174430911102464X. Epub 2011 Jul 27.
Cytochrome P450 (CYP) enzymes constitute a large family of haemoproteins that catalyze the monooxygenation of a great variety of endogenous and exogenous organic compounds. In common with other members of the CYP153 family of alkane hydroxylases, CYP153C1 from the oligotrophic bacterium Novosphingobium aromaticivorans DSM 12444 can bind linear alkanes such as heptane, octane and nonane. Here, the production, purification and crystallization of CYP153C1 and the collection of high-resolution diffraction data to 1.77 Å resolution are reported. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 61.0, b = 96.3, c = 149.8 Å, α = β = γ = 90.0°. Preliminary X-ray diffraction data analysis revealed that the asymmetric unit is most likely to contain two protein molecules.
细胞色素P450（CYP）酶构成了一个庞大的血红素蛋白家族，可催化多种内源性和外源性有机化合物的单加氧反应。与CYP153烷烃羟化酶家族的其他成员一样，来自贫营养细菌新鞘氨醇菌DSM 12444的CYP153C1可以结合直链烷烃，如庚烷、辛烷和壬烷。本文报道了CYP153C1的制备、纯化和结晶以及分辨率达到1.77 Å的高分辨率衍射数据的收集。晶体属于空间群P2(1)2(1)2(1)，晶胞参数为a = 61.0、b = 96.3、c = 149.8 Å，α = β = γ = 90.0°。初步的X射线衍射数据分析表明，不对称单元很可能包含两个蛋白质分子。
