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.
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