Crystallization and preliminary X-ray analysis of the C-terminal RNase III domain of human Dicer

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 62; no. 4; pp. 402 - 404
• Main Authors: Takeshita, Daijiro, Zenno, Shuhei, Lee, Woo Cheol, Nagata, Koji, Saigo, Kaoru, Tanokura, Masaru
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Blackwell Publishing Ltd 01.04.2006; International Union of Crystallography
• Subjects: Cloning, Molecular; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; Crystallization Communications; CRYSTALS; Dicer protein; DIFFUSION; Humans; MOLECULES; Peptide Fragments - chemistry; Peptide Fragments - genetics; Peptide Fragments - isolation & purification; PROTEINS; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; RESOLUTION; Ribonuclease III - chemistry; Ribonuclease III - genetics; Ribonuclease III - isolation & purification; RNase III domains; SOLVENTS; SPACE GROUPS; X-Ray Diffraction
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S174430910600889X

Human Dicer protein contains two RNase III domains (RNase IIIa and RNase IIIb) which are involved in the production of short interfering RNAs (siRNAs). The C‐terminal RNase III domain (RNase IIIb) of human Dicer was expressed, purified and crystallized by the sitting‐drop vapour‐diffusion method. The crystals belonged to space group C2221, with unit‐cell parameters a = 88.6, b = 199.7, c = 119.6 Å, and diffracted X‐rays to 2.0 Å resolution. The asymmetric unit contained three molecules of the RNase IIIb and the solvent content was 67%.