Crystallization and preliminary crystallographic analysis of type 1 RNase H from the hyperthermophilic archaeon Sulfolobus tokodaii 7.
Crystallization and preliminary crystallographic studies of type 1 RNase H from the hyperthermophilic archaeon Sulfolobus tokodaii 7 were performed. A crystal was grown at 277 K by the sitting-drop vapour-diffusion method. Native X-ray diffraction data were collected to 1.5 angstroms resolution using synchrotron radiation from station BL41XU at SPring-8. The crystal belongs to space group P4(3), with unit-cell parameters a = b = 39.21, c = 91.15 angstroms. Assuming the presence of one molecule in the asymmetric unit, the Matthews coefficient V(M) was calculated to be 2.1 angstroms3 Da(-1) and the solvent content was 40.5%. The structure of a selenomethionine Sto-RNase HI mutant obtained using a MAD data set is currently being analysed.
You
Dong Ju
DJ
Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Chon
Hyongi
H
Koga
Yuichi
Y
Takano
Kazufumi
K
Kanaya
Shigenori
S
D019843:Archaeal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D001483:Base Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D017931:DNA Primers; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D016914:Ribonuclease H / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D016944:Sulfolobus / Q000201:enzymology*; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D017931:DNA Primers; D011994:Recombinant Proteins; D016914:Ribonuclease H; C078856:ribonuclease HI