CRYSTALLIZATION AND 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 Marek BORKOVCOVÁ Petra JANDA Lubomír HEJÁTKO Jan
Year of publication	2009
Type	Conference abstract
MU Faculty or unit	Faculty of Science
Citation
Description	The receiver domain (RD) of a sensor histidine kinase (HKs) catalyses transphosphorylation reaction during the action of HKs in hormonal and abiotic signalling in plants. Crystals of the recombinant RD of the Arabidopsis HK CYTOKININ-INDEPENDENT1 (CKI1RD) have been obtained by the hanging-drop vapour-diffusion method using ammonium sulphate as a precipitant. The crystals diffracted at beamline BW7B of the DORIS-III storage ring to approx. 2.4A. The diffraction has been improved significantly - to at least 2.0A - after applying of a non-water cryoprotectant. The crystals belong to space group C2221 with unit-cell parameters a=54.46, b=99.82, c=79.94 A, the asymmetric unit contains one molecule of the protein. The structure of CKI1RD had been solved by a molecular-replacement.
Related projects:	Molecular basis of cell and tissue regulations Regulation of morphogenesis of plant cells and organs