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Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi , the causative agent of Chagas' disease
Author(s) -
Krauth-Siegel R.Luise,
Sticherling Christian,
Jöst Ingrid,
Walsh Christopher T.,
Pai Emil F.,
Kabsch Wolfgang,
Lantwin Christina B.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81501-p
Subject(s) - monoclinic crystal system , polyethylene glycol , dimer , crystallization , trypanosoma cruzi , chemistry , chagas disease , crystallography , tetragonal crystal system , stereochemistry , resolution (logic) , monomer , crystal structure , biochemistry , biology , organic chemistry , polymer , parasite hosting , artificial intelligence , immunology , world wide web , computer science
Trypanothione reductase from Trypanosoma cruzi is the most promising target molecule for the rational design of a specific drug against Chagas' disease. The recombinant protein was purified in a single Chromatographie step and crystallized. Two crystal forms suitable for X‐ray diffraction analysis were obtained. Tetragonal crystals ( a = b = 87.4 Å, c = 152.3 Å) were grown from 30% polyethylene glycol (average M r = 8,000) in the presence of 0.2% β‐ n ‐octylglucoside (space group either P4 2 with one dimer or P4 2 22 with one monomer in the asymmetric unit). Monoclinic crystals (space group P2, a = 136.3 Å, b = 91.1 Å, c = 126.0 Å, β = 94°) were grown from 1.2 M sodium citrate in the presence of 2% octanoyl‐ N ‐methyl‐glucamide. They contain two dimers of the enzyme in the asymmetric unit; both crystal forms diffract to 3 Å resolution.