Open AccessCrystallization and preliminary X‐ray diffraction analysis of a glutathione S ‐transferase from Xylella fastidiosa
Author(s) -
Garcia Wanius,
Travensolo Regiane F.,
Rodrigues Nathalia C.,
Muniz João R. C.,
Caruso Célia S.,
Lemos Eliana G. M.,
Araujo Ana Paula U.,
Carrilho Emanuel
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910706825x
Subject(s) - glutathione , crystallization , glutathione transferase , triclinic crystal system , chemistry , escherichia coli , glutathione s transferase , affinity chromatography , isozyme , resolution (logic) , transferase , chromatography , biochemistry , crystallography , enzyme , crystal structure , organic chemistry , gene , artificial intelligence , computer science
Glutathione S ‐transferases (GSTs) form a group of multifunctional isoenzymes that catalyze the glutathione‐dependent conjugation and reduction reactions involved in the cellular detoxification of xenobiotic and endobiotic compounds. GST from Xylella fastidiosa ( xf GST) was overexpressed in Escherichia coli and purified by conventional affinity chromatography. In this study, the crystallization and preliminary X‐ray analysis of xf GST is described. The purified protein was crystallized by the vapour‐diffusion method, producing crystals that belonged to the triclinic space group P 1. The unit‐cell parameters were a = 47.73, b = 87.73, c = 90.74 Å, α = 63.45, β = 80.66, γ = 94.55°. xf GST crystals diffracted to 2.23 Å resolution on a rotating‐anode X‐ray source.