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. 2021 May 24;13(1):1922134. doi: 10.1080/19420862.2021.1922134

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© 2021 Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Cryo-electron microscopy of Fab-spike trimer complexes. (a) Binding of CR3022-B6 Fab (blue) to SARS-CoV-2 trimer (gray with RBD highlighted in salmon). A single Fab molecule bound to the RBD domain of a spike protomer in the ‘up’ conformation was resolved. (b) Binding of CR3014-D1 Fab (green) to SARS-CoV-2 trimer (gray with RBD highlighted in salmon). Both antibody Fab bound with similar stoichiometry (with two protomers in the ‘down’ and one in the ‘up’ conformation), and epitope specificity (overlapping with the ACE2 binding interface)