Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis

Yogesh B. Khandokar, Avinash Londhe, Shilpa Patil, Jade K Forwood

Research output: Contribution to journalArticleOtherpeer-review

3 Citations (Scopus)


Neisseria meningitidis is the causative microorganism of many human diseases, including bacterial meningitis; together with Streptococcus pneumoniae, it accounts for approximately 80% of bacterial meningitis infections. The emergence of antibiotic-resistant strains of N. meningitidis has created a strong urgency for the development of new therapeutics, and the high-resolution structural elucidation of enzymes involved in cell metabolism represents a platform for drug development. Acetyl-CoA hydrolase is involved in multiple functions in the bacterial cell, including membrane synthesis, fatty-acid and lipid metabolism, gene regulation and signal transduction. Here, the first recombinant protein expression, purification and crystallization of a hexameric acetyl-CoA hydrolase from N. meningitidis are reported. This protein was crystallized using the hanging-drop vapour-diffusion technique at pH 8.5 and 290K using ammonium phosphate as a precipitant. Optimized crystals diffracted to 2.0Å resolution at the Australian Synchrotron and belonged to space group P213 (unit-cell parameters a = b = c = 152.2Å), with four molecules in the asymmetric unit.

Original languageEnglish
Pages (from-to)1303-1306
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number11
Publication statusPublished - Nov 2013
Externally publishedYes


  • Acetyl-CoA hydrolase
  • Hotdog fold
  • Neisseria meningitidis
  • Thioesterase

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