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 126.96.36.199). 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 language||English (US)|
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - Dec 1 2002|
ASJC Scopus subject areas
- Structural Biology