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. Author manuscript; available in PMC: 2021 Jan 17.
Published in final edited form as: ACS Synth Biol. 2020 Jan 7;9(1):125–131. doi: 10.1021/acssynbio.9b00411

Figure 2.

Figure 2.

Structural view of potential epistatic interactions between F and G libraries. (A) Pentameric complex between F and G shown in surface view. For both F and G, one monomer is detailed as a ribbon color-coded according to the saturation mutagenesis library prepared in this work. (B) Close-up of interaction surface between the F3 sublibrary of F protein (green ribbons) and G2 sublibrary of G protein (purple spheres). (C) Distance mapping between alpha carbons in F and G crystal structure. Residues within 10 Å are colors red, 10–20 are black, and >20 are blue. Euclidian distances calculated from F–G crystal structure. Heatmap shows that many opportunities exist for close proximity (interactions) both within and between fragments.