TY - JOUR
T1 - Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila
AU - Siddiqui, Tanzeela
AU - Paxman, Jason John
AU - Dogovski, Con
AU - Panjikar, Santosh
AU - Perugini, Matthew Anthony
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
UR - http://www.ncbi.nlm.nih.gov/pubmed/24100576
U2 - 10.1107/S1744309113024639
DO - 10.1107/S1744309113024639
M3 - Article
SN - 1744-3091
VL - 69
SP - 1177
EP - 1181
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
IS - 10
ER -