Fig. 1: Strep-Tsa1 and His6-Tsa2 form hetero-oligomers in E. coli.
From: Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins
a, Purification scheme and WB analysis of the eluates from tandem-affinity copurifications of Strep-Tsa1 and His6-Tsa2 with Ni-NTA agarose, followed by StrepTactin agarose or vice versa. Eluate samples were separated by reducing SDS–PAGE. The calculated molecular masses of Strep-Tsa1 and His6-Tsa2 are 22.9 kDa and 23.8 kDa, respectively. Uncropped blots are shown in Supplementary Fig. 1. b, Tandem-affinity copurification of Strep-Tsa1ΔCR and His6-Tsa2. Protein samples were treated with NEM to block free thiols and separated by nonreducing SDS–PAGE to preserve intersubunit disulfide bonds, as shown in b. In a and b, gels are representative of those obtained during three experimental repeats, each yielding similar results. M, marker; FT, flow through; W, wash; E, eluate.
