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  • Title: Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.
    Author: Siddiqui T, Paxman JJ, Dogovski C, Panjikar S, Perugini MA.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Oct; 69(Pt 10):1177-81. PubMed ID: 24100576.
    Abstract:
    Dihydrodipicolinate synthase (DHDPS) catalyses the rate-limiting step in the biosynthesis of meso-diaminopimelate and lysine. Here, the cloning, expression, purification and crystallization of DHDPS from the intracellular pathogen Legionella pneumophila are described. Crystals grown in the presence of high-molecular-weight PEG precipitant and magnesium chloride were found to diffract beyond 1.65 Å resolution. The crystal lattice belonged to the hexagonal space group P6₁22, with unit-cell parameters a=b=89.31, c=290.18 Å, and contained two molecules in the asymmetric unit. The crystal structure was determined by molecular replacement using a single chain of Pseudomonas aeruginosa DHDPS as the search model.
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