Crystallization and preliminary X-ray diffraction study of thermostable RNase HIII from Bacillus stearothermophilus.
A thermostable ribonuclease HIII from Bacillus stearothermophilus (Bst RNase HIII) was crystallized and preliminary crystallographic studies were performed. Plate-like overlapping polycrystals were grown by the sitting-drop vapour-diffusion method at 283 K. Native X-ray diffraction data were collected to 2.8 A resolution using synchrotron radiation from station BL44XU at SPring-8. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 66.73, b = 108.62, c = 48.29 A. Assuming one molecule per asymmetric unit, the VM value was 2.59 A3 Da(-1) and the solvent content was 52.2%.
Chon
Hyongi
H
Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Matsumura
Hiroyoshi
H
Koga
Yuichi
Y
Takano
Kazufumi
K
Kanaya
Shigenori
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification; D017356:Synchrotrons; D013816:Thermodynamics; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D012260:Ribonucleases; C117079:ribonuclease HIII