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

ABSTRACT: 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.

SUBMITTER: Sheng J

PROVIDER: S-EPMC2330212 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature

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

Sheng Ju J Ye Jun J Rosen Barry P BP

Acta crystallographica. Section F, Structural biology and crystallization communications 20070312 Pt 4

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 b ...[more]

PMID: 17401194

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