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

Tanzeela Siddiqui, Jason John Paxman, Con Dogovski, Santosh Panjikar, Matthew Anthony Perugini

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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 A resolution. The crystal lattice belonged to the hexagonal space group P6(1)22, with unit-cell parameters a=b=89.31, c=290.18 A, 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.
Original languageEnglish
Pages (from-to)1177 - 1181
Number of pages5
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number10
Publication statusPublished - 2013

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