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. Author manuscript; available in PMC: 2021 Sep 21.
Published in final edited form as: Sci Signal. 2020 Jul 7;13(639):eaax6313. doi: 10.1126/scisignal.aax6313

Fig. 6. Both WT and triple-cysteine-mutant (C32A/C236A/C196A) AtFN3K exist as two distinct species in solution, and the WT dimer is redox sensitive.

Fig. 6.

(A) Size exclusion chromatography (SEC) of AtFN3K WT protein. Each fraction was 1 ml in volume. A: aggregates, D: dimer, M: monomer. (B) PK/LDH assay using 1 μg of protein to assess the activity of WT protein in the presence or absence of 2 mM DTT. Ribulose-N-α-Ac-lysine was used as the substrate. Data are means ± standard error of six independent experiments. (C and D) As in (A) and (B), respectively, for the triple-cysteine-mutant protein.