Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.

Glutaredoxin 2 (Grx2) from Escherichia coli is larger in size than classical glutaredoxins. It is extremely efficient in the catalysis of reduced glutathione-dependent disulfide reduction. A complex of Grx2 with reduced glutathione (GSH) has been crystallized. Data were collected to 1.60 A. The crystals belong to space group P3(2)21, with one Grx2-GSH complex in the asymmetric unit. The unit-cell parameters are a = b = 50.10, c = 152.47 A. A Grx2 mutant, C9S/C12S, which cannot form a disulfide bond with GSH was also crystallized. The crystals diffracted to 2.40 A and belong to space group P2(1)2(1)2(1), with one molecule in the asymmetric unit. The unit-cell parameters are a = 28.16, b = 78.65, c = 89.16 A.

Citation

Ju Sheng, Jun Ye, Barry P Rosen. Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione. Acta crystallographica. Section F, Structural biology and crystallization communications. 2007 Apr 01;63(Pt 4):280-2

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PMID: 17401194

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