TY - JOUR
T1 - Crystallization and preliminary crystallographic analysis of a new class of glutathione transferase from nematodes
AU - Hao, Q.
AU - Schuller, D. J.
AU - Barrett, John
AU - Brophy, Peter M.
AU - Campbell, Alison Mary
AU - Kriksunov, I. A.
N1 - 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.
PY - 2003
Y1 - 2003
N2 - 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).
AB - 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).
U2 - 10.1107/S0907444903009041
DO - 10.1107/S0907444903009041
M3 - Article
SN - 0907-4449
VL - 59
SP - 1262
EP - 1264
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 7
ER -