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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 4(69), p. 408-411, 2013

DOI: 10.1107/s1744309113003989

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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the mitochondrial tryparedoxin peroxidase fromLeishmania braziliensis

This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

Tryparedoxin peroxidase (TXNPx) is an essential constituent of the main enzymatic scavenger system for reactive oxygen species (ROS) in trypanosomatids. Genetic studies have demonstrated the importance of this system for the development and virulence of these parasites, representing a potential target for the discovery of new trypanocidal drugs. In this work, the mitochondrial TXNPx fromLeishmania braziliensiswas cloned, overexpressed, purified and crystallized. The crystals diffracted to 3.3 Å resolution and belonged to space groupP42212, with unit-cell parametersa=b= 131.8,c= 44.4 Å. These studies will contribute to a better understanding of the molecular mechanisms involved in ROS detoxification by trypanosomatids.