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Can you comment on the time scale of the morphing between the pro-capsid form and the mature virion form?
Would it be possible to fluorescently label only a small fraction of the molecules of interest, so that you can look at higher concentrations relevant for assembly but still have very single bursts of fluorescence?
The Forster distances of 55 angstroms in the FRET seems quite large. Could you give a rough idea of the 'size' of an individual monomer, and the size of the final assembled virion?
Can you get cryoEM structures of the mutant forms you used? You showed that the mutants still assemble into mature structures, but it would be interesting to see if any structural changes take place.
Yes, thank you!
Thank you SiYu!
The retained enzyme in the wiffle ball constructs, you mentioned might be retained via aggregation. Have you confirmed the aggregability of the enzymes you are using? Do they naturally self-associate? Do we see aggregates of the proteins outside of these nano-constructs?
Have you looked at scaffolding protein exit with your charge mutants?
Thank you @Trevor, wonderful work. Does the disordered portion in the non-truncated components assume induced structure in the final assembled particle?
Hi Miranda - thanks. We have no information about the ordering of the scaffolding protein inside - unfortunately.
Is the stress accumulated around the pentagonal defects?
Great session, thanks to the organizers!
Thank you so much for attending and your great questions!
Thanks everyone for the great session!
Thank you for the great session!
Stephen E. Moore