Crystallization and preliminary X-ray diffraction studies of catalase-peroxidase from Synechococcus PCC 7942.
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.
Wada
Kei
K
Research Institute for Advanced Science and Technology, Osaka Prefecture University, Sakai, Osaka 599-8570, Japan. keiwada@biochem.osakafu-u.ac.jp
Tada
Toshiji
T
Nakamura
Yoshihiro
Y
Kinoshita
Takayoshi
T
Tamoi
Masahiro
M
Shigeoka
Shigeru
S
Nishimura
Keiichiro
K
D001426:Bacterial Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D000458:Cyanobacteria / Q000201:enzymology*; D010544:Peroxidases / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D010544:Peroxidases; C081610:catalase-peroxidase, bacteria