Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana.

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Authors

KLUMPLER Tomáš PEKÁROVÁ Blanka MAREK Jaromír BORKOVCOVÁ Petra JANDA Lubomír HEJÁTKO Jan

Year of publication 2009
Type Article in Periodical
Magazine / Source Acta Crystallographica Section F
MU Faculty or unit

Faculty of Science

Citation
Field Genetics and molecular biology
Keywords receiver domains; two-component systems; histidine kinases; cytokinins; phosphorelay; CKI1
Description The receiver domain (RD) of a sensor histidine kinase (HK) catalyses the transphosphorylation reaction during the action of HKs in hormonal and abiotic signalling in plants. Crystals of the recombinant RD of the Arabidopsis thaliana HK CYTOKININ-INDEPENDENT1 (CKI1RD) have been obtained by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant and glycerol as a cryoprotectant. The crystals diffracted to approximately 2.4 A resolution on beamline BW7B of the DORIS-III storage ring. The diffraction improved significantly after the use of a non-aqueous cryoprotectant. Crystals soaked in Paratone-N diffracted to at least 2.0 A resolution on beamline BW7B and their mosaicity decreased more than tenfold. The crystals belonged to space group C2221, with unit-cell parameters a = 54.46, b = 99.82, c = 79.94 A. Assuming the presence of one molecule of the protein in the asymmetric unit gives a Matthews coefficient VM of 2.33 A3 Da-1. A molecular-replacement solution has been obtained and structure refinement is in progress.
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