Open AccessCrystallization and preliminary X‐ray diffraction analysis of dihydrodipicolinate synthase 2 from Arabidopsis thaliana
Author(s) -
Griffin Michael D. W.,
Billakanti Jagan M.,
Gerrard Juliet A.,
Dobson Renwick C. J.,
Pearce F. Grant
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111033276
Subject(s) - arabidopsis thaliana , crystallization , crystallography , x ray crystallography , diffraction , materials science , chemistry , physics , biochemistry , optics , gene , organic chemistry , mutant
Dihydrodipicolinate synthase (DHDPS; EC 4.2.1.52) catalyzes the first committed step of the lysine‐biosynthetic pathway in plants and bacteria. Since ( S )‐lysine biosynthesis does not occur in animals, DHDPS is an attractive target for rational antibiotic and herbicide design. Here, the cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of DHDPS2 from Arabidopsis thaliana are reported. Diffraction‐quality protein crystals belonged to space group P 2 1 2 1 2.