FEBS Letters | |
Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease | |
Krauth-Siegel, R.Luise1  Jöst, Ingrid1  Lantwin, Christina B.2  Kabsch, Wolfgang2  Pai, Emil F.3  Sticherling, Christian1  Walsh, Christopher T.4  | |
[1] Institut für Biochemie II, Universität Heidelberg, Im Neuenheimer Feld 328, D-6900 Heidelberg, Germany;Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung, Jahnstrasse 29, D-6900 Heidelberg, Germany;Departments of Biochemistry and Molecular and Medical Genetics, University of Toronto, 1 Kings's College Circle, Toronto, Ont., M5S 1A8, Canada;Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA | |
关键词: 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; | |
DOI : 10.1016/0014-5793(93)81501-P | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
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