Open AccessCloning, overexpression, purification and preliminary X‐ray analysis of the catalytic domain of the ethylene receptor ETR1 from Arabidopsis thaliana
Author(s) -
Panneerselvam Saravanan,
Kaljunen Heidi,
MuellerDieckmann Jochen
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911302842x
Subject(s) - arabidopsis thaliana , ethylene , cloning (programming) , arabidopsis , domain (mathematical analysis) , catalysis , chemistry , biophysics , crystallography , biology , biochemistry , gene , computer science , mutant , programming language , mathematical analysis , mathematics
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 I 222 or I 2 1 2 1 2 1 with one molecule per asymmetric unit. They diffracted X‐ray radiation to beyond 1.85 Å resolution.