Cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium Bartonella henselae strain Houston-1 at 2.1?A resolution.

ABSTRACT: The enzyme dihydrodipicolinate synthase catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis. Dihydrodipicolinate synthase catalyzes the condensation of L-aspartate 4-semialdehyde and pyruvate to synthesize L-2,3-dihydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the pathogenic bacterium Bartonella henselae, the causative bacterium of cat-scratch disease, are presented. Protein crystals were grown in conditions consisting of 20%(w/v) PEG 4000, 100?mM sodium citrate tribasic pH 5.5 and were shown to diffract to ?2.10?Å resolution. They belonged to space group P212121, with unit-cell parameters a = 79.96, b = 106.33, c = 136.25?Å. The final R values were Rr.i.m. = 0.098, Rwork = 0.183, Rfree = 0.233.

SUBMITTER: Naqvi KF 

PROVIDER: S-EPMC4708043 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature