Wada Kei, Tada Toshiji, Nakamura Yoshihiro, Kinoshita Takayoshi, Tamoi Masahiro, Shigeoka Shigeru, Nishimura Keiichiro
Research Institute for Advanced Science and Technology, Osaka Prefecture University, Sakai, Osaka 599-8570, Japan.
Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):157-9. doi: 10.1107/s0907444901017735. Epub 2001 Dec 21.
The recombinant catalase-peroxidase of Synechococcus PCC 7942 overexpressed in Escherichia coli was purified and crystallized by the hanging-drop vapour-diffusion method using sodium formate as a precipitant. The crystals belonged to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 109.3, c = 202.0 A. The calculated V(M) value based on a dimer in the asymmetric unit was 1.9 A(3) Da(-1). A native data set was collected to 2.3 A resolution from a frozen crystal using synchrotron radiation at SPring-8.
在大肠杆菌中过表达的聚球藻PCC 7942重组过氧化氢酶-过氧化物酶,以甲酸钠作为沉淀剂,通过悬滴气相扩散法进行纯化和结晶。晶体属于四方晶系空间群P4(1)2(1)2或P4(3)2(1)2,晶胞参数a = b = 109.3,c = 202.0 Å。基于不对称单元中的二聚体计算的V(M)值为1.9 ų Da⁻¹。使用SPring-8的同步辐射从冷冻晶体收集了分辨率为2.3 Å的天然数据集。