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. Author manuscript; available in PMC: 2021 Feb 11.
Published in final edited form as: Nature. 2020 May 27;583(7814):150–153. doi: 10.1038/s41586-020-2333-6

Extended Data Table 1. Cryo-EM statistics for map and model refinement.

Pre-Fusion pH8 (EMDB-10696) (PDB 6Y5G) Pre-Fusion pH5 (EMDB-10697) (PDB 6Y5H) Dilated Form 1 (EMDB-10698) (PDB 6Y5I) Dilated Form 2 (EMDB-10699) (PDB 6Y5J) Full Extended HA2 (EMDB-10700) (PDB 6Y5K) Subtracted Extended HA2 (EMDB-10701) (PDB 6Y5L) Post Fusion (EMDB-10702)
State Number - I II III IV IV V
Timepoint - 20 s 10 s 20 s 20 s 20 s 30 min + 2-ME
Data collection and processing
Magnification 75 000 75 000 75 000 75 000 75 000 75 000 75 000
Voltage (kV) 300 300 300 300 300 300 300
Electron exposure (e–/Å2) 33.9 33.9 33.9 33.9 33.9 33.9 33.9
Defocus range (μm) 1.5-3 1.5-3 1.5-3 1.5-3 1.5-3 1.5-3 1.5-3
Pixel size (Å) 1.09 1.09 1.09 1.09 1.09 1.09 1.09
Symmetry imposed C3 C3 Cl Cl C3 C3 C3
Initial particle images (no.) 643 k 1.39 M 1.53 M 1.39 M 1.39 M 1.39 M 2.24 M
Final particle images (no.) 200 k 157 k 72 k 124 k 189 k 546 k 62 k
Map resolution (Å) 3.0 3.0 5.5 5.6 4.2 3.6 9.9
    FSC threshold 0.143
Refinement Software CryoSPARC CryoSPARC CryoSPARC CryoSPARC CryoSPARC CryoSPARC RELION
Map resolution range (Å) 2.6-3.4 2.6-3.4 5-9 5-9 3-5 3-7 -
Refinement
Initial model used (PDB code) 2YPG 2YPG 2YPG 2YPG 2YPG&1QU1 2YPG&1QU1 -
Map sharpening B factor (Å2) -172 -170 -283 -322 -170 -225 -
Model composition
    Non-hydrogen atoms 12036 11994 11928 9609 10617 3855 -
    Protein residues 1470 1470 1470 1185 1335 477
R.m.s. deviations
    Bond lengths (Å) 0.005 0.004 0.004 0.005 0.005 0.004 -
    Bond angles (°) 0.553 0.959 0.987 1.000 1.049 0.999
Validation
    MolProbity score 1.48 1.35 1.54 1.82 1.65 1.78 -
    Clashscore 3.69 2.81 4.31 10.88 10.23 5.46 -
    Poor rotamers (%) 0.94 0.70 0.47 0.94 0 0 -
Ramachandran plot
    Favored (%) 95.4 95.9 95.3 96.2 97.35 92.16 -
    Allowed (%) 4.6 4.1 4.7 3.8 2.65 7.84 -
    Disallowed (%) 0 0 0 0 0 0 -
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