Open AccessCrystallization and preliminary X‐ray diffraction study of thermostable RNase HIII from Bacillus stearothermophilus
Author(s) -
Chon Hyongi,
Matsumura Hiroyoshi,
Koga Yuichi,
Takano Kazufumi,
Kanaya Shigenori
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105003659
Subject(s) - orthorhombic crystal system , crystallography , rnase p , crystallization , x ray crystallography , synchrotron radiation , materials science , diffraction , crystal structure , chemistry , physics , optics , rna , biochemistry , organic chemistry , gene
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 Å resolution using synchrotron radiation from station BL44XU at SPring‐8. The crystals belong to the orthorhombic space group P 2 1 2 1 2, with unit‐cell parameters a = 66.73, b = 108.62, c = 48.29 Å. Assuming one molecule per asymmetric unit, the V M value was 2.59 Å 3 Da −1 and the solvent content was 52.2%.