Open AccessCrystallization and preliminary X‐ray diffraction analysis of the flax cytokinin oxidase LuCKX1.1
Author(s) -
Wan Li,
Williams Simon J.,
Zhang Xiaoxiao,
Ericsson Daniel J.,
Koeck Markus,
Dodds Peter N.,
Ellis Jeffrey G.,
Kobe Bostjan
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113023142
Subject(s) - cytokinin , crystallization , oxidase test , chemistry , crystallography , diffraction , x ray crystallography , biochemistry , enzyme , optics , organic chemistry , physics , auxin , gene
The plant hormones cytokinins play a central role in regulating cell division and developmental events. Cytokinin oxidase regulates the levels of these plant hormones by catalyzing their irreversible oxidation, which contributes to the regulation of various morpho‐physiological processes controlled by cytokinins. In this study, the crystallization and preliminary X‐ray diffraction analysis of the flax cytokinin oxidase LuCKX1.1 are reported. Plate‐like crystals of LuCKX1.1 were obtained using PEG 3350 as a precipitant and diffracted X‐rays to 1.78 Å resolution. The protein crystals have the symmetry of space group C 2 and are most likely to contain two molecules per asymmetric unit.