Extended Data Fig. 3: Cryo-EM data processing and validation for C144–S, C002–S and C121–S complexes. | Nature

Extended Data Fig. 3: Cryo-EM data processing and validation for C144–S, C002–S and C121–S complexes.

From: SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies

Extended Data Fig. 3

ai, Representative micrograph selected from total dataset (Supplementary Table 2), 2D class averages, gold-standard Fourier shell correlation (FSC) plots, and local resolution estimations for C144–S 6P (ac), C002–S 2P (df) and C121–S 2P (gi). Scale bars, 100 nm. For the C002–S dataset, two classes were resolved: state 1, C002 Fabs bound to three down RBDs, and state 2, C002 Fabs bound to two down and one up RBD. For the C121–S 2P dataset, two classes were resolved: state 1, C121 Fabs bound to two down and one up RBD and state 2, C121 Fabs bound to one down, two up RBDs.

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