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.Základní údaje
Originální název
Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana.
Název česky
Cloning, purification, crystallization and preliminary X-ray analysis of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana.
Autoři
KLUMPLER, Tomáš; Blanka PEKÁROVÁ ORCID; Jaromír MAREK ORCID; Petra BORKOVCOVÁ; Lubomír JANDA a Jan HEJÁTKO ORCID
Vydání
Acta Crystallographica Section F, 2009, 1744-3091
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
Genetika a molekulární biologie
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 0.551
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:14310/09:00036140
Organizační jednotka
Přírodovědecká fakulta
UT WoS
Klíčová slova anglicky
receiver domains; two-component systems; histidine kinases; cytokinins; phosphorelay; CKI1
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 23. 8. 2010 10:35, prof. 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.
Česky
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.
Návaznosti
| LC06034, projekt VaV |
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| MSM0021622415, záměr |
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