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Acta Crystallogr F Struct Biol Commun. 2016 Jan;72(Pt 1):2-9. doi: 10.1107/S2053230X15023213. Epub 2016 Jan 1.

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 information

1
Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, 85 Lomb Memorial Drive, Rochester, NY 14623-5603, USA.
2
Seattle Structural Genomics Center for Infectious Disease, USA.
3
Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch, New Zealand.
4
Berkeley Center for Structural Biology, Ernest Orlando Lawrence Berkeley National Laboratory, USA.

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.

KEYWORDS:

Bartonella henselae; cat-scratch disease; diaminopimelate; dihydrodipicolinate synthase; lysine biosynthesis

PMID:
26750477
PMCID:
PMC4708043
DOI:
10.1107/S2053230X15023213
[Indexed for MEDLINE]
Free PMC Article

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