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. 2018 Jan 11;7:e31522. doi: 10.7554/eLife.31522

Figure 3. Complexes of MukF N- and C-terminal domains with MukB head variants.

Binding and stoichiometry of complexes was determined by SEC-MALS. (A) Left panel; MukBHN (red), 2FN2 (blue), and MukBHN + 2FN2 (green) at a 1:1.25 monomer:dimer molar ratio. Middle panel; MukBH (pink), 2FN2 (blue), and MukBH + 2FN2 (brown) at 1:0.25 m:d ratio. Right panel; MukBH (pink), FC2 (lime green), and MukBH + FC2 (green) at a 1:1 m:m ratio. (B) MukBHN (red), 2FN6 (grey), and MukBHN + 2FN6 (blue) at a 1:0.25 m:d ratio. (C) MukBHN + 2FN2 at a1:1 m:d ratio (dark green), and MukBHN + 2FN2 + FC2 at a 1:1:1 m:d:m ratio (olive green).

Figure 3.

Figure 3—figure supplement 1. SEC-MALS analysis of MukBHN-2FN2 complexes.

Figure 3—figure supplement 1.

The samples contained a mixture of MukBHN and FN2 at ratios of; 3:1 m:d, pink; and 0.3:1 m:d, purple.
Figure 3—figure supplement 2. SEC-MALS analysis of MukBHN–2FN2 and MukBHN–2FN2–FC2 complexes in the absence and presence of ATP (1 mM).

Figure 3—figure supplement 2.

Figure 3—figure supplement 3. Binding affinities of MukF fragments to MukB.

Figure 3—figure supplement 3.

(A) FCS measurements of FN2 and FN10 binding to MukB. Cy5 labelled fragments were at a fixed ~10 nM concentration; exponential fits to data points were used to extract Kds. Error bars represent S.D. of three independent experiments. (B) FPA measurements of FN3 and FC2 binding to MukB. Cy5 labelled FN3 and FC2 fragments were at concentrations 5 nM and 9 nM, respectively.
Figure 3—figure supplement 3—source data 1. Binding affinities of MukF fragments to MukB.
elife-31522-fig3-figsupp3-data1.xlsx (8.7KB, xlsx)
DOI: 10.7554/eLife.31522.009