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

无乳链球菌双功能γ-谷氨酰半胱氨酸合成酶-谷氨酰半胱氨酸合成酶的结晶及初步晶体学分析

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Abstract

gamma-Glutamylcysteine synthetase-glutathione synthetase (gammaGCS-GS) is a bifunctional enzyme that catalyzes two consecutive steps of ATP-dependent peptide formation in glutathione biosynthesis. Streptococcus agalactiae gammaGCS-GS is a target for the development of potential therapeutic agents. gammaGCS-GS was crystallized using the sitting-drop vapour-diffusion method. The crystals grew to dimensions of 0.3 x 0.2 x 0.2 mm under reducing conditions with 5 mM TCEP. X-ray data were collected to 2.8 A resolution from a tetragonal crystal that belonged to space group I4(1).

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