Crystallization and preliminary X-ray analysis of PH1566, a putative ribosomal RNA-processing factor from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
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 A resolution using a synchrotron-radiation source. The space group of the crystals was determined as primitive orthorhombic P2(1)2(1)2(1), with unit-cell parameters a = 45.9, b = 47.4, c = 95.7 A. The crystals contain one molecule in the asymmetric unit (VM = 2.5 A3 Da(-1)) and have a solvent content of 50%.
Jia
Min Ze
MZ
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Tokyo 113-8657, Japan.
Ohtsuka
Jun
J
Lee
Woo Cheol
WC
Nagata
Koji
K
Tanokura
Masaru
M
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D043902:Pyrococcus horikoshii / Q000737:chemistry* / Q000235:genetics; D012323:RNA Processing, Post-Transcriptional; D012335:RNA, Ribosomal / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; C484364:DIM2 protein, S cerevisiae; D012335:RNA, Ribosomal; D029701:Saccharomyces cerevisiae Proteins