Table 1.

Cryoelectron Microscopy (Cryo-EM) and Modeling Results

Cryo-EM Data Collection, Refinement, and Validation Statistics
		C1 Virion Capsid (EMDB: EMD-20430)	C1 Portal Vertex (EMDB: EMD-20431)	C5 Portal Vertex (EMDB: EMD-20432, PDB: 6PPB)	C12 Portal (EMDB: EMD-20437, PDB: 6PPI)	C1 Penton Vertex Register, CATC-Absent (EMDB: EMD-20433, PDB: 6PPD)	C1 Penton Vertex Register, CATC-Binding (EMDB: EMD-20436, PDB: 6PPH)
Data Collection and Processing
Magnification		14,000	14,000	14,000	14,000	14,000	14,000
Voltage (kV)		300	300	300	300	300	300
Electron exposure (e−/Å2)		25	25	25	25	25	25
Defocus range (μm)		−1 to −3	−1 to −3	−1 to −3	−1 to −3	−1 to −3	−1 to −3
Pixel size (Å)		2.06	1.03	1.03	1.03	1.03	1.03
Symmetry imposed		C1	C1	C5	C12	C1	C1
Initial particle images (no.)		44,328	44,328	44,328	44,328	44,328	44,328
Final particle images (no.)		39,073	39,073	39,773	39,073	1,521,505 (sub-particles)	928,740 (sub-particles)
Map resolution (Å)		7.6	5.2	4.3	4.7	3.7	3.8
	FSC threshold	0.143	0.143	0.143	0.143	0.143	0.143
Estimated resolution range (Å)		7.0-8.5	4.0-6.0	3.5-5.5	3.5-5.5	3.5-4.8	3.5-4.8
Map sharpening B factor (Å2)		0.0	180.5	177.4	200.0	177.4	180.4
Model refinement
Model-to-map fit, mask CC		N/A	N/A	0.787	0.798	0.765	0.769
Model Composition
	Non-hydrogen atoms			62,671	39,504	68,769	73,502
	Protein residues			7,953	4,956	8,728	9,326
	Ligands			N/A	N/A	N/A	N/A
Mean Isotropic B Factor (Å2)
	Protein			50.49	204.94	40.81	33.40
	Ligand			N/A	N/A	N/A	N/A
Root-Mean-Square Deviations
	Bond lengths (Å)			0.005	0.003	0.008	0.007
	Bond angles (°)			0.923	0.680	1.043	1.014
Validation
	MolProbity score			1.55	1.54	1.63	1.60
	Clashscore			4.23	4.21	4.78	4.79
	Rotamer outliers (%)			0.31%	0.00%	0.64%	0.49%
Ramachandran Statistics
	Outliers (%)			0.11%	0.00%	0.20%	0.17%
	Allowed (%)			4.92%	4.89%	5.42%	4.85%
	Favored (%)			94.97%	95.11%	94.38%	94.97%

The table shows cryo-EM data collection, reconstruction, and model validation results and values. See also Figures S1 and S2.