Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila

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 angstrom resolution. The crystal lattice belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 89.31, c = 290.18 angstrom, 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.