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Crystallographic Studies of Triosephosphate Isomerase from Schistosoma mansoni.

Authors :
Jimenez-Sandoval P
Castro-Torres E
Diaz-Quezada C
Brieba LG
Source :
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2020; Vol. 2151, pp. 211-218.
Publication Year :
2020

Abstract

Protein structure determination by X-ray crystallography guides structure-function and rational drug design studies. Helminths cause devastating diseases, including schistosomiasis that affects over one-third of the human population. Trematodes from the genus Schistosoma heavily depend on glycolysis; thus enzymes involved in this metabolic pathway are potential drug targets. Here we present a protocol to obtain crystal structures of recombinantly expressed triosephosphate isomerase from S. mansoni (SmTPI) that diffracted in house to a resolution of 2 Å.

Details

Language :
English
ISSN :
1940-6029
Volume :
2151
Database :
MEDLINE
Journal :
Methods in molecular biology (Clifton, N.J.)
Publication Type :
Academic Journal
Accession number :
32452007
Full Text :
https://doi.org/10.1007/978-1-0716-0635-3_17