Table 1 Cryo-EM structure quality indicators.

Data collection and processing	Empty particle	Full virion	Open particle C5	Open particle C1
Magnification	130,000	130,000	130,000	130,000
Voltage (kV)	300	300	300	300
Exposure (e^–.Å^–2)	36	36	36	36
Pixel size (Å)	1.079	1.079	1.079	1.079
Symmetry	I4	I4	C5	C1
Init. No of particles	72705	72705	72705	72705
Fin. No of particles	17702	1748	1120	1120
Map resolution (Å)	2.9	3.7	10	12
FSC threshold	0.143	0.143	0.143	0.143
Refinement
Software	RELION 3.1	RELION 3.1	RELION 3.1	RELION 3.1
Initial model	de novo	Empty particle	Empty particle	Empty particle
Model composition and quality
Atoms (except hydrogens)	10414^a	10414^a	112191^b	112191^b
Residues	1316^a	1316^a	14181^b	14181^b
B-factors
Protein (asymmetric unit)	30.01	65.16	N/A^c	N/A^c
R.M.S. deviations
Bond length (Å)	0.0022	0.0022^d	0.0022^d	0.0022^d
Bond angles (°)	1.2455	1.2455^d	1.2455^d	1.2455^d
Validation
MolProbity score (percentile)	1.08 (^100th)	1.08 (^100th)^d	1.08 (^100th)^d	1.08 (^100th)^d
ClashScore (percentile)	0.34 (^100th)	0.34 (^100th)^d	0.34 (^100th)^d	0.34 (^100th)^d
Poor Rotamers (%)	0.79	0.79^d	0.79^d	0.79^d
Ramachandran plot
Outliers (%)	0	0^d	0^d	0^d
Favored (%)	92.68	92.68^d	92.68^d	92.68^d
Accession codes
PDB	7QWX	7QWZ	7ZUF	7ZTS
EMDB	EMD-14194	EMD-14195	EMD-14975	EMD-14963

^aNumber of atoms or residues in icosahedral asymmetric unit.
^bNumber of atoms or residues in eleven icosahedral asymmetric units forming one-fifth of the particle. The icosahedral asymmetric unit forming the border of the opening contains fewer resolved residues than those from the remainder of the capsid.
^cB-factors were not refined because of the limited resolution of the cryo-EM reconstruction.
^dProtein geometry was refined against the reconstruction of the empty particle. The structures of capsid proteins from the empty particle were fitted into the other reconstructions.

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