Cloning, expression, purification and preliminary X-ray crystallographic studies of 2-methylisocitrate lyase from Salmonella typhimurium

Dhirendra K. Simanshu, P. S. Satheshkumar, S. Parthasarathy, H. S. Savithri, M. R.N. Murthy

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Abstract

In Salmonella typhimurium, propionate is oxidized to pyruvate via the 2-methylcitric acid cycle. The last step of this cycle, the cleavage of 2-methylisocitrate to succinate and pyruvate, is catalysed by 2-methylisocitrate lyase (EC 4.1.3.30). Methylisocitrate lyase (molecular weight 32 kDa) with a C-terminal polyhistidine affinity tag has been cloned and overexpressed in Escherichia coli and purified and crystallized under different conditions using the hanging-drop vapour-diffusion technique. Crystals belong to the orthogonal space group P212121, with unit-cell parameters a = 63.600, b = 100.670, c = 204.745 Å. A complete data set to 2.5 Å resolution has been collected using an image-plate detector system mounted on a rotating-anode X-ray generator.

Original languageEnglish (US)
Pages (from-to)2159-2161
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number12
DOIs
Publication statusPublished - Dec 1 2002

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ASJC Scopus subject areas

  • Structural Biology

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