Extended Data Fig. 7: Cryo-EM analysis of antibody 2-4 in complex with the S trimer.

a, Representative micrograph and CTF of the micrograph. 8,324 micrographs were collected in total. b, Representative 2D class averages. c, Resolution of the consensus map with C3 symmetry as calculated by 3DFSC. d, The local resolution of the full map as calculated by cryoSPARC at an FSC cutoff of 0.5. e, Representative density of the Fab 2-4 (blue) and RBD (green) interface, showing interactions of CDR H3 in red, L1 in magenta, and L3 in light magenta (left), along with CDR H2 and the N-linked glycosylation added by SHM at ASN58 (right). f, Fab 2-4 binding interface with RBD. V_H is shown in blue, V_L in light blue, with CDRs H1 in orange, H2 in yellow, H3 in red, L1 in magenta, and L3 in light magenta. g, Positions of antibodies 2-4, S309⁸, and BD-23⁹ on the trimeric CoV-2 spike. h, Antibody BD-23⁹ in complex with S trimer. i, Somatic hypermutations found only in the antibody 2-4 heavy chain, shown in brown. The mutation A60T creates an NxT sequence leading to N58 glycosylation.