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. Author manuscript; available in PMC: 2017 Jul 18.
Published in final edited form as: Nature. 2017 Jan 18;541(7638):488–493. doi: 10.1038/nature21049

Extended data figure 5. Exposure of AimR to SAIRGA peptide reduces propensity for dimerization.

Extended data figure 5

Purified AimR was eluted from a gel-filtration column, dialyzed, then mixed with SAIRGA peptide (f.c. 100 µM) dissolved in water or with equal amount of volume without peptide and incubated at room temperature for 5 minutes. The protein samples were then mixed for 30 minutes with different concentrations of the crosslinker BS3 bis(sulfosuccinimidyl)suberate. Presented are electrophoresis results analyzed using the TapeStation instrument (Agilent Technologies), showing that in the absence of peptide, purified AimR tends to preferentially be cross linked into dimers, whereas in the presence of the SAIRGA peptide, dimerization is significantly reduced.