title: 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.
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Hubert
authors.initials: H
authors.lastname: Mayerhofer
authors.forename: Christoph
authors.initials: C
authors.lastname: Mueller-Dieckmann
authors.forename: Jochen
authors.initials: J
authors.lastname: Mueller-Dieckmann
mesh_terms: D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D029681:Arabidopsis Proteins; D011494:Protein Kinases; C477753:CTR1 protein, Arabidopsis