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.