Open AccessCloning, expression, purification and preliminary X‐ray analysis of the protein kinase domain of constitutive triple response 1 (CTR1) from Arabidopsis thaliana
Author(s) -
Mayerhofer Hubert,
MuellerDieckmann Christoph,
MuellerDieckmann Jochen
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110047640
Subject(s) - arabidopsis thaliana , mutant , protein kinase domain , arabidopsis , kinase , protein kinase a , resolution (logic) , biology , chemistry , microbiology and biotechnology , crystallography , biochemistry , gene , artificial intelligence , computer science
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 P 4 1 2 1 2 and P 4 2 2 1 2, respectively, with two molecules per asymmetric unit in both cases.