FIGURE 3.

Analysis of the DsbA-peptide crystal. a, analysis by SDS-PAGE (lane ii) revealed that approximately half of the EcDsbA in the crystal had formed a covalent complex with the peptide. The peptide-DsbA complex (lane iii) was clearly resolved from free EcDsbA (lane iv) under the conditions used to run the gel. (Molecular weight markers are shown in lane i.) b, ribbon diagram of EcDsbA (Protein Data Bank code 3DKS, chain C). Each of the four molecules in the asymmetric unit adopted a typical DsbA fold comprising a thioredoxin (blue) and α-helical (magenta) domains and the insertion points (orange). The sulfur atoms of the active site cysteine residues are shown in yellow CPK representation.