title: Crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase 2 from Arabidopsis thaliana.
abstract: 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 P2(1)2(1)2.
authors.affiliation: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 30 Flemington Road, Parkville, Victoria 3010, Australia. mgriffin@unimelb.edu.au
authors.forename: Michael D W
authors.initials: MD
authors.lastname: Griffin
authors.forename: Jagan M
authors.initials: JM
authors.lastname: Billakanti
authors.forename: Juliet A
authors.initials: JA
authors.lastname: Gerrard
authors.forename: Renwick C J
authors.initials: RC
authors.lastname: Dobson
authors.forename: F Grant
authors.initials: FG
authors.lastname: Pearce
mesh_terms: D017360:Arabidopsis / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006836:Hydro-Lyases / Q000737:chemistry*
chemical_list: D006836:Hydro-Lyases; C020040:4-hydroxy-tetrahydrodipicolinate synthase
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