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. 2022 Feb 1;603(7902):706–714. doi: 10.1038/s41586-022-04474-x

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© The Author(s) 2022

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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Extended Data Fig. 1 — a. Variant structures for Delta and Omicron of spike protein displaying mutational sites in red colour, generated using the cryo-EM structure PDB# 7A94 as a reference. The schematic highlights differences in domain-wise mutations across protein length. b. Side and top down surface representation of the Omicron spike protein. Spike homotrimer structures were created predicted in silico by the Alphafold2 software package. Individual mutations making up the Omicron spike are highlighted in red on each of the three homotrimers.