title: Cloning, overexpression, purification and preliminary X-ray analysis of the catalytic domain of the ethylene receptor ETR1 from Arabidopsis thaliana.
abstract: Ethylene is a gaseous plant hormone which controls many aspects of plant growth and development. It is perceived by membrane-bound receptors with a similarity to bacterial two-component systems. The catalytic and ATP-binding domain of the histidine kinase domain of ETR1 from Arabidopsis thaliana has been cloned, overexpressed and crystallized. The protein was crystallized together with various nucleotides. Crystals obtained in the presence of ADP belonged to space group I222 or I2(1)2(1)2(1) with one molecule per asymmetric unit. They diffracted X-ray radiation to beyond 1.85 Å resolution.
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, 22603 Hamburg, Germany.
authors.forename: Saravanan
authors.initials: S
authors.lastname: Panneerselvam
authors.forename: Heidi
authors.initials: H
authors.lastname: Kaljunen
authors.forename: Jochen
authors.initials: J
authors.lastname: Mueller-Dieckmann
mesh_terms: D017360:Arabidopsis / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: D029681:Arabidopsis Proteins; C494590:ETR1 protein, Arabidopsis; D011956:Receptors, Cell Surface
keywords: Arabidopsis thaliana; ETR1