Abstract
The last enzyme in the arginine-biosynthesis pathway, argininosuccinate lyase, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized, and preliminary X-ray studies have been carried out on the crystals. The His-tagged tetrameric enzyme with a subunit molecular weight of 50.9kDa crystallized with two tetramers in the asymmetric unit of the orthorhombic unit cell, space group P212121. Molecular-replacement calculations and self-rotation calculations confirmed the space group and the tetrameric nature of the molecule. © 2013 International Union of Crystallography.
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Paul, A., Mishra, A., Surolia, A., & Vijayan, M. (2013). Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(12), 1422–1424. https://doi.org/10.1107/S1744309113031138
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