Extended Data Fig. 1: Characterization of the materials for purification of the TEF30-PSII complexes.
a, The recombinant CrTEF30 protein purified through the cobalt affinity chromatography was analyzed with SDS-PAGE. The expression cassette of recombinant CrTEF30 with 3×Flag and 6×His tags fused at the N-terminal region is shown at bottom. The experiment was repeated independently three times with similar results. b, Images showing the fluorescence of mVenus (colored in green) and chlorophyll (colored in red) from the TEF30-ox cells were recorded with a confocal microscope. The bright field and the merged images are displayed in the bottom row. The experiment was repeated independently three times with similar results. c, Immunodetection of endogenous native TEF30 in the SDG fractions. Thylakoids from the wild type (WT) cells grown under low-light (20 μmol photons m−2 s−1) and high-light (330 μmol photons m−2 s−1) conditions were solubilized with α-DDM and separated through the SDG ultracentrifugation. The SDG fractions were extracted and the endogenous native TEF30 proteins were analyzed using SDS-PAGE and western blot with anti-CrTEF30 antibodies. Note that all TEF30 is from the endogenous source of the WT cells and no exogenous TEF30 was added to the sample. LHCII-M, LHCII monomer; LHCII-T, LHCII trimer.
