Table 1.

Comparison of Structures Based On Stabilization Strategy.

	Virus Name	Capsid Size	Triangulation Number	Johnson Fold	Basis of Chainmail	Chainmail Type	Resolving Method
HK97 like	HK97	660 Å	T=7	HK97-like	Isopeptide bonds	Covalent	X-ray Crystallography (3.44 Å)
P-22 like	φ29	450 Å wide	prolate T=3 Q=5	HK97-like	BIG2-like domain	Non-covalent	cryoEM (7.9 Å)
		540 Å wide
	P-22	690 Å	T=7	HK97-like	I-domian	Non-covalent	capsid: cryoEM (4.0 Å), I-domain: NMR
	Sf6	690 Å	T=7	HK97-like	I-domian	Non-covalent	cryoEM (7.8 Å)
	CUS-3	690 Å	T=7	HK97-like	I-domian	Non-covalent	cryoEM (6.8 Å)
	T4	860 Å wide	prolate Tend = 13	HK97-like	I-domian	Non-covalent	gp24: X-ray Crystallography (2.9 Å), capsid: cryoEM (22 Å)
		1200 Å long	laevo Tmid=20
BPP-1 like	BPP-1	670 Å	T=7	BPP-1-like	Auxiliary Protein Dimer	Non-covalent	cryoEM (3. 5 Å)
	ε15	n/a	T=7	BPP-1-like	Auxiliary Protein Dimer	Non-covalent	cryoEM(4.5 Å)
Lambda like	Phage λ	600 Å	T=7	HK97-like	Auxiliary Protein Trimer	Non-covalent	gpd: X-ray Crystallography (1.1 Å), capsid: cryoEM (6.8 Å)
	80α	630 Å	T=7	HK97-like	Auxiliary Protein Trimer	Non-covalent	cryoEM (10.2 Å)
More Complex	SIO-2	800 Å	T=12	HK97-like	Auxiliary Proteins	Non-covalent	cryoEM(8.5 Å)
	RRV (herpesvirus)	1200 Å	T=16	HK97-like	Triplex hetero-trimers, dimerization domains,	Non-covalent	cryoEM (7.2 Å)
	φRSL1	1230 Å	T=27	HK97-like	Auxiliary Protein Trimer, Spike complex bridge between Trimers	Non-covalent	cryoEM (9 Å)