ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

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

Simanshu , DK and Satheshkumar , PS and Parthasarathy , S and Savithri , HS and Murthy , MR (2002) Cloning, expression, purification and preliminary X-ray crystallographic studies of 2-methylisocitrate lyase from Salmonella typhimurium. Acta Crystallogr. In: Acta Crystallographica Section D Biological Crystallography, 58 (12). pp. 2159-2161.

[img] PDF
vj0057.pdf - Published Version
Restricted to Registered users only

Download (240Kb) | Request a copy
Official URL: http://scripts.iucr.org/cgi-bin/paper?S09074449020...

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 P2(1)2(1)2(1), with unit-cell parameters a = 63.600, b = 100.670, c = 204.745 Angstrom. A complete data set to 2.5 Angstrom resolution has been collected using an image-plate detector system mounted on a rotating-anode X-ray generator.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to International Union of Crystallography .
Keywords: propionate catabolism; 2-methylisocitrate lyase.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 14 Dec 2010 06:30
Last Modified: 14 Dec 2010 06:30
URI: http://eprints.iisc.ernet.in/id/eprint/34031

Actions (login required)

View Item View Item