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. 2021 Nov 2;12:6304. doi: 10.1038/s41467-021-26539-7

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a, b Cryo-EM densities for 13G9 Fab (antigen binding fragment)-S (a; 3.9 Å) and 58G6 Fab-S (b; 3.6 Å) complexes, revealing binding of 13G9 or 58G6 to RBDs in the all ‘up’ state. c Superimposition of RBD-hACE2 [Protein Data Bank (PDB) ID 6LZG][https://www.rcsb.org/structure/6LZG] complex structure together with RBD-13G9 Fab (left) or RBD-58G6 Fab (right) variable domains, respectively. d Alignment of 13G9 and 58G6 Fabs on the same RBD. HC, heavy chain; LC, light chain. CDR, complementarity determining region.