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Crystallization and preliminary X‐ray diffraction study of thermostable RNase HIII from Bacillus stearothermophilus

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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 P21212, 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 Å3 Da−1 and the solvent content was 52.2%.
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Keywords: ribonuclease HIII

Document Type: Research Article

Publication date: March 1, 2005

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