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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 Å resolution
Author(s) -
Naqvi Kubra F.,
Staker Bart L.,
Dobson Renwick C. J.,
Serbzhinskiy Dmitry,
Sankaran Banumathi,
Myler Peter J.,
Hudson André O.
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15023213
Subject(s) - crystallization , atp synthase , peptidoglycan , cloning (programming) , biosynthesis , biology , biochemistry , chemistry , enzyme , crystallography , microbiology and biotechnology , stereochemistry , organic chemistry , computer science , programming language
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 m M sodium citrate tribasic pH 5.5 and were shown to diffract to ∼2.10 Å resolution. They belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 79.96, b = 106.33, c = 136.25 Å. The final R values were R r.i.m. = 0.098, R work = 0.183, R free = 0.233.