Initiating a crystallographic study of trypanothione reductase

William N. Hunter, Keith Smith, Zygmunt Derewenda, Stephen J. Harrop, Jarjis Habash, M. S. Islam, John R. Helliwell, Alan H. Fairlamb

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


We have obtained well-ordered single crystals of the flavoenzyme trypanothione reductase from Crithidia fasciculata. The crystals are tetragonal rods with unit cell dimensions a = 128·6 Å, c = 92·5 Å. The diffraction pattern corresponds to a primitive lattice, Laue class 4/m. Diffraction to better than 2·4 Å has been recorded at the Daresbury Synchrotron. The accurate elucidation of the three-dimensional structure of this enzyme is required to support the rational design of compounds active against a variety of tropical diseases caused by trypanosomal parasites.

Original languageEnglish
Pages (from-to)235-237
Number of pages3
JournalJournal of Molecular Biology
Issue number2
Publication statusPublished - 20 Nov 1990

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


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