Crystallization and preliminary crystallographic analysis of a new class of glutathione transferase from nematodes

Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1262-4. doi: 10.1107/s0907444903009041. Epub 2003 Jun 27.


Mouse and Heligmosomoides polygyrus constitute a readily manipulated small-animal laboratory model for investigating host-nematode interactions. Two major forms of glutathione transferase (GST) are expressed in H. polygyrus adult worms following primary infection. One of these forms belongs to a new class of GST which has only been found in the nematode phylum and therefore presents a possible target for nematode control. In this study, crystals were obtained of a recombinant representative of this new GST class from H. polygyrus. These crystals belong to the triclinic space group P1, with unit-cell parameters a = 72.7, b = 74.0, c = 88.6 A, alpha = 79.1, beta = 80.1, gamma = 81.5 degrees, and are likely to contain four homodimers in the asymmetric unit. X-ray diffraction data were collected to 1.8 A resolution on station A1 at the Cornell High-Energy Synchrotron Source (CHESS).

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray / methods
  • Glutathione Transferase / chemistry*
  • Helminth Proteins / chemistry*
  • Nematoda / enzymology*
  • Nematospiroides dubius / enzymology
  • Recombinant Proteins


  • Helminth Proteins
  • Recombinant Proteins
  • Glutathione Transferase