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


ABSTRACT: 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%.

SUBMITTER: Jia MZ 

PROVIDER: S-EPMC2150936 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

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

Jia Min Ze MZ   Ohtsuka Jun J   Lee Woo Cheol WC   Nagata Koji K   Tanokura Masaru M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20051216 Pt 1


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 a  ...[more]

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