Open AccessPurification, crystallization and preliminary X‐ray analysis of glutathione peroxidase Gpx3 from Saccharomyces cerevisiae
Author(s) -
Yang Zhu,
Zhou CongZhao
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106017829
Subject(s) - gpx3 , saccharomyces cerevisiae , peroxidase , chemistry , gpx1 , monomer , glutathione peroxidase , crystallization , gpx6 , crystallography , glutathione , biochemistry , yeast , enzyme , organic chemistry , polymer
The glutathione peroxidase Gpx3 from the yeast Saccharomyces cerevisiae has been overexpressed, purified and crystallized. Both gel‐filtration and dynamic light‐scattering (DLS) results indicate that Gpx3 is a monomer in solution at a concentration of about 2 mg ml −1 , whereas glutathione peroxidases are normally tetrameric or dimeric. X‐ray diffraction data from a single crystal of Gpx3 have been collected to 2.6 Å resolution. The crystals are triclinic and belong to space group P 1, with unit‐cell parameters a = 38.187, b = 43.372, c = 56.870 Å, α = 71.405, β = 73.376, γ = 89.633°. There are two Gpx3 monomers in a crystallographic asymmetric unit. Preliminary analyses show that the yeast Gpx3 is quite different from those of mammals.