Publication details
CRYSTALLIZATION AND X-RAY ANALYSIS OF THE RECEIVER DOMAIN OF THE HISTIDINE KINASE CKI1 FROM ARABIDOPSIS THALIANA
| Authors | |
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| Year of publication | 2009 |
| Type | Conference abstract |
| MU Faculty or unit | |
| 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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