Crystallization and preliminary crystallographic analysis of bifunctional -glutamylcysteine synthetase-glutatione synthetase from Streptococcus agalactiae

Abstract

-Glutamylcysteine synthetase-glutathione synthetase (GCS-GS) is a bifunctional enzyme that catalyzes two consecutive steps of ATP-dependent peptide formation in glutathione biosynthesis. Streptococcus agalactiae GCS-GS is a target for the development of potential therapeutic agents. GCS-GS was crystallized using the sitting-drop vapour-diffusion method. The crystals grew to dimensions of 0.3 0.2 0.2 mm under reducing conditions with 5 mM TCEP. X-ray data were collected to 2.8 Å resolution from a tetragonal crystal that belonged to space group I41. © 2009 International Union of Crystallography All rights reserved.