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. 2013 May 29;69(Pt 6):704–709. doi: 10.1107/S1744309113011470

Figure 1.

Figure 1

Production of ρ-Da1a. The recombinant protein (molecular mass 27 487 Da) consisted of a fusion with the ZZ domain of protein A, a histidine tag and a TEV protease cleavage site. The fusion protein is produced in inclusion bodies, with a yield of 30–50 mg per litre of culture. (a) SDS–PAGE of the different fractions obtained during the production and purification of Gly-ρ-Da1a-K34A. Lanes 1 and 6, molecular-weight markers (labelled in kDa). Lanes 2 and 3, band at molecular mass 30 kDa corresponding to the fusion protein obtained after induction by 1 mM IPTG for 3 h at 310 K. Lane 4, elution of Gly-ρ-Da1a-K34A after TEV protease cleavage. Lane 5, elution of the TEV and fusion protein with 300 mM imidazole. (b) HPLC purification of Gly-ρ-Da1a-K34A after oxidation in folding buffer. (c) HPLC purification of the oxidized s-ρ-Da1a obtained from solid-phase peptide synthesis. Relevant peaks are marked with arrows.