Cloning, expression, purification, crystallization and preliminary crystallographic analysis of selenomethionine-labelled KaiC-like protein PH0186 from Pyrococcus horikoshii OT3
- Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657 (Japan)
Preliminary crystallographic analysis of KaiC-like protein PH0186 from Pyrococcus horikoshii OT3 is reported. KaiC is the central protein in the circadian-clock system of cyanobacteria. A selenomethionine-labelled KaiC-homologous protein from Pyrococcus horikoshii OT3 (PH0186; 28 kDa) was crystallized by the sitting-drop vapour-diffusion method using ethanol as a 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 to be C2, with unit-cell parameters a = 173.7, b = 51.8, c = 97.5 Å, β = 122.8°. The crystal contains three molecules in the asymmetric unit (V{sub M} = 2.2 Å{sup 3} Da{sup −1}) and has a solvent content of 43.5%. Sixfold noncrystallographic symmetry was identified from self-rotation calculations, assuming the presence of a hexamer in the crystal.
- OSTI ID:
- 22360316
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 4; Other Information: PMCID: PMC2330226; PMID: 17401208; PUBLISHER-ID: pu5180; OAI: oai:pubmedcentral.nih.gov:2330226; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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