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Cloning, expression, purification and preliminary X-ray analysis of the protein kinase domain of constitutive triple response 1 (CTR1) from Arabidopsis thaliana.

ABSTRACT: Ethylene, a gaseous plant hormone, is perceived by a group of membrane-bound receptors. Constitutive triple response 1 (CTR1) from Arabidopsis thaliana directly interacts with ethylene receptors and thus links signal reception to the intracellular signalling pathway. The C-terminal protein kinase domain of CTR1 has been crystallized in its wild-type form and as a kinase-dead mutant. The wild-type crystals diffracted X-ray radiation to 3?Å resolution and the crystals of the kinase-dead mutant diffacted to 2.5?Å resolution. The crystals belonged to space groups P4(1)2(1)2 and P4(2)2(1)2, respectively, with two molecules per asymmetric unit in both cases.

SUBMITTER: Mayerhofer H

PROVIDER: S-EPMC3079988 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Cloning, expression, purification and preliminary X-ray analysis of the protein kinase domain of constitutive triple response 1 (CTR1) from Arabidopsis thaliana.

Mayerhofer Hubert H Mueller-Dieckmann Christoph C Mueller-Dieckmann Jochen J

Acta crystallographica. Section F, Structural biology and crystallization communications 20101223 Pt 1

Ethylene, a gaseous plant hormone, is perceived by a group of membrane-bound receptors. Constitutive triple response 1 (CTR1) from Arabidopsis thaliana directly interacts with ethylene receptors and thus links signal reception to the intracellular signalling pathway. The C-terminal protein kinase domain of CTR1 has been crystallized in its wild-type form and as a kinase-dead mutant. The wild-type crystals diffracted X-ray radiation to 3 Å resolution and the crystals of the kinase-dead mutant dif ...[more]

PMID: 21206040

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