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  Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease

Krauth-Siegel, R. L., Sticherling, C., Jöst, I., Walsh, C. T., Pai, E. F., Kabsch, W., et al. (1993). Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease. FEBS Letters, 317(1-2), 105-108. doi:10.1016/0014-5793(93)81501-P.

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Genre: Journal Article
Alternative Title : Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease

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FEBSLett_317_1993_105.pdf (Any fulltext), 424KB
 
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 Creators:
Krauth-Siegel, R. Luise, Author
Sticherling, Christian, Author
Jöst, Ingrid, Author
Walsh, Christopher T., Author
Pai, Emil F., Author
Kabsch, Wolfgang1, 2, Author              
Lantwin, Christina B.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Trypanothione reductase; Drug design; Chagas' disease; Flavoprotein; Protein crystallography; Trypanosoma cruzi; GSH; glutathione; GSSG; glutathione disulfide; TR; trypanothione reductase; TS2 ; trypanothione disulfide; T(SH)2 ; trypanothione
 Abstract: 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 P42 with one dimer or P4222 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.

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Language(s): eng - English
 Dates: 1992-12-072001-11-121993-02-08
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 317 (1-2) Sequence Number: - Start / End Page: 105 - 108 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501