15 February 2023 1 9K Report

Hi,

This is probably a very naive question,

but I see that a lot of Cryo-EM structure uses FAB to stabilize the conformation or to increase the size of the protein to solve its structure.

How can you argue that the structure solved when it was bound to FAB is physiologically relevant? For example, if your protein is a transporter, how do you know that binding of FAB to the protein of interest didn't induce any conformational changes that don't occur during the transport cycle in vivo?

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