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

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dc.contributor.author Hao, Q.
dc.contributor.author Schuller, D. J.
dc.contributor.author Barrett, John
dc.contributor.author Brophy, Peter M.
dc.contributor.author Campbell, Alison M.
dc.contributor.author Kriksunov, I. A.
dc.date.accessioned 2010-03-09T15:38:26Z
dc.date.available 2010-03-09T15:38:26Z
dc.date.issued 2003
dc.identifier.citation Hao , Q , Schuller , D J , Barrett , J , Brophy , P M , Campbell , A M & Kriksunov , I A 2003 , ' Crystallization and preliminary crystallographic analysis of a new class of glutathione transferase from nematodes ' Acta Crystallographica Section D Biological Crystallography , vol 59 , no. 7 , pp. 1262-1264 . , 10.1107/S0907444903009041 en
dc.identifier.issn 0907-4449
dc.identifier.other PURE: 137879
dc.identifier.other dspace: 2160/4215
dc.identifier.uri http://hdl.handle.net/2160/4215
dc.description Kriksunov, I. A., Schuller, D. J., Campbell, A. M., Barrett, J., Brophy, P. M., Hao, Q. (2003). Crystallization and preliminary crystallographic analysis of a new class of glutathione transferase from nematodes.   Acta Crystallographica Section D-Biological Crystallography, 59, (7), 1262-1264. en
dc.description.abstract 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 Å, = 79.1, = 80.1, = 81.5°, and are likely to contain four homodimers in the asymmetric unit. X-ray diffraction data were collected to 1.8 Å resolution on station A1 at the Cornell High-Energy Synchrotron Source (CHESS). en
dc.format.extent 3 en
dc.language.iso eng
dc.relation.ispartof Acta Crystallographica Section D Biological Crystallography en
dc.title Crystallization and preliminary crystallographic analysis of a new class of glutathione transferase from nematodes en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1107/S0907444903009041
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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