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. 2014 Aug 19;26(8):3435–3448. doi: 10.1105/tpc.114.125930

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Figure 3. — Purification of the b₆f Complex from the b₆f-ΔpetP Mutant.

(A) Elution profile from a preparative IEC column (second purification step): peak 0, with b₆f degradation forms; peak 1, b₆f-monomer; peak 2, b₆f-dimer. UnoQ1 (Bio-Rad), 0.5 mL/min, 4°C; gradient 1: 0 to 4.2 mM NaCl, gradient 2: 4.2 to 8.2 mM NaCl, gradient 3: 8 0.2 to 20 mM NaCl.

(B) SDS-PAGE (silver-stained) of fractions from chromatography: (1) IMAC of b₆f-ΔPetP, (2) peak 0 of IEC, (3) peak 1 of IEC, and (4) peak 2 of IEC.

(C) Immunoblot analysis of Cyt b₆f-ΔPetP: (1) Cyt b₆f-ΔPetP-peak of IMAC, (2) IEC fraction 1 (b₆f monomer), (3) IEC fraction 2 (b₆f dimer), and (4) PetP heterologously expressed in E. coli as reference (synthetic peptide-antibody; Davids Biotechologie).

(D) BN-PAGE (silver-stained) of isolated b₆f-ΔPetP- and WT b₆f-complex: (1) b₆f-ΔPetP after IMAC, (2) IEC fraction 1 (b₆f-ΔPetP monomer), (3) IEC fraction 2 (b₆f-ΔPetP dimer), (4) b₆f after IMAC, (5) IEC fraction 1 (b₆f monomer), and (6) IEC fraction 2 (b₆f dimer); for details, see text.