Detailed Information on Publication Record
2009
Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana.
KLUMPLER, Tomáš, Blanka PEKÁROVÁ, Jaromír MAREK, Petra BORKOVCOVÁ, Lubomír JANDA et. al.Basic information
Original name
Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana.
Name in Czech
Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana.
Authors
KLUMPLER, Tomáš (203 Czech Republic, guarantor), Blanka PEKÁROVÁ (203 Czech Republic), Jaromír MAREK (203 Czech Republic), Petra BORKOVCOVÁ (203 Czech Republic), Lubomír JANDA (203 Czech Republic) and Jan HEJÁTKO (203 Czech Republic)
Edition
Acta Crystallographica Section F, 2009, 1744-3091
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
Genetics and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 0.551
RIV identification code
RIV/00216224:14310/09:00036140
Organization unit
Faculty of Science
UT WoS
000265639600012
Keywords in English
receiver domains; two-component systems; histidine kinases; cytokinins; phosphorelay; CKI1
Tags
International impact, Reviewed
Změněno: 23/8/2010 10:35, doc. RNDr. Jan Hejátko, Ph.D.
V originále
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.
In Czech
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.
Links
| LC06034, research and development project |
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| MSM0021622415, plan (intention) |
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