Crystallization and preliminary X-ray analysis of PH1566, a putative ribosomal RNA-processing factor from the hyperthermophilic archaeon Pyrococcus horikoshii OT3

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2006-01, Vol.62 (1), p.47-48
• Main Authors: Jia, Min Ze, Ohtsuka, Jun, Lee, Woo Cheol, Nagata, Koji, Tanokura, Masaru
• Format: Article
• Language: English
• Subjects: Archaeal Proteins - chemistry; Archaeal Proteins - genetics; Archaeal Proteins - metabolism; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; Crystallization Communications; Crystallography, X-Ray; CRYSTALS; DIFFUSION; MOLECULES; PH1566; PROCESSING; Pyrococcus horikoshii; Pyrococcus horikoshii - chemistry; Pyrococcus horikoshii - genetics; RESOLUTION; RNA Processing, Post-Transcriptional; RNA, Ribosomal - genetics; RNA, Ribosomal - metabolism; RNA-processing factors; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Sequence Homology, Amino Acid; SOLVENTS; SPACE GROUPS
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309105040613

A putative ribosomal RNA‐processing factor consisting of two KH domains from Pyrococcus horikoshii OT3 (PH1566; 25 kDa) was crystallized by the sitting‐drop vapour‐diffusion method using PEG 3000 as the precipitant. The crystals diffracted X‐rays to beyond 2.0 Å resolution using a synchrotron‐radiation source. The space group of the crystals was determined as primitive orthorhombic P212121, with unit‐cell parameters a = 45.9, b = 47.4, c = 95.7 Å. The crystals contain one molecule in the asymmetric unit (VM = 2.5 Å3 Da−1) and have a solvent content of 50%.