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Expression, purification, crystallization and preliminary X-ray analysis of the KaiC-like protein PH0187 from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.

ABSTRACT: KaiC is the central protein in the circadian rhythm in cyanobacteria. The 28?kDa KaiC-like protein PH0187 from the hyperthermophilic archaeon Pyrococcus horikoshii was expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method at 293?K. Crystals of PH0187 were obtained using a reservoir solution consisting of 1.0?M ammonium phosphate monobasic and 0.1?M sodium citrate tribasic pH 5.3 (the final pH value of the reservoir solution was 4.8) and diffracted X-rays to 2.75?Å resolution. The crystal of PH0187 belonged to space group P6(3)22, with unit-cell parameters a=b=239.1, c=106.5?Å. The crystal contained four PH0187 molecules in the asymmetric unit.

SUBMITTER: Kang HJ

PROVIDER: S-EPMC3079995 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray analysis of the KaiC-like protein PH0187 from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.

Kang Hee-Jin HJ Kubota Keiko K Miyazono Ken-ichi K Tanokura Masaru M

Acta crystallographica. Section F, Structural biology and crystallization communications 20101224 Pt 1

KaiC is the central protein in the circadian rhythm in cyanobacteria. The 28 kDa KaiC-like protein PH0187 from the hyperthermophilic archaeon Pyrococcus horikoshii was expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method at 293 K. Crystals of PH0187 were obtained using a reservoir solution consisting of 1.0 M ammonium phosphate monobasic and 0.1 M sodium citrate tribasic pH 5.3 (the final pH value of the reservoir solution was 4.8) and diffracte ...[more]

PMID: 21206047

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