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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 2.1Å resolution

  • Author(s): Naqvi, KF
  • Staker, BL
  • Dobson, RCJ
  • Serbzhinskiy, D
  • Sankaran, B
  • Myler, PJ
  • Hudson, AO
  • et al.

Published Web Location

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4708043/
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Abstract

© 2016 International Union of Crystallography. 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, 100mM sodium citrate tribasic pH 5.5 and were shown to diffract to ∼2.10Å resolution. They belonged to space group P212121, with unit-cell parameters a = 79.96, b = 106.33, c = 136.25Å. The final R values were R r.i.m. = 0.098, R work = 0.183, R free = 0.233.

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