Fig. 1: Biochemical characteristics of DENV soluble E with stabilizing mutations (sE SC).

A Cartoon depiction of recombinant E homodimers with monomers (gray, colored) in head-to-tail orientation. Mutation sets at the dimer interface (I2, I9), domain I/II hinge (U6, S1) and domain I core (P4) increased protein production and homodimer affinity. These mutations were applied to DENV1-4 sE to obtain stable dimers for all four serotypes. B Mass photometry histograms of DENV sE WT and SC at 50 nM and room temperature. C Summary of yield and dimer stability of DENV sE. Yields and mass photometry data for DENV sE WT were obtained from (²⁹, Figs. 2A and 3A), yields for DENV sE SC are from small scale and large-scale expressions in Expi293F; nd = no data, as we were unable to produce enough DENV1 sE WT for analysis.