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The mature empty capsid of phage HK97 is composed of 420 protein units in an icosahedral T=7 lattice. The subunits are covalently linked into fiveand six-membered rings through a lysine-asparagine cross-link. These rings are topologically linked, connecting all 420 subunits into a single stable unit. The coat protein has a unique fold and consists of two domains and two extended regions responsible for a complicated pattern of interactions in the mature capsid. The protein shell undergoes large conformational changes during particle maturation. In the mature shell, there are only few differences in the quasi-equivalent five-fold and six-fold interactions, while the capsids initially are formed by skewed hexamers. We have now refined the crystal structure of the mature capsids to 3.44 Å resolution to analyze the interactions between the subunits and correlate this with the low-resolution structures of the intermediates in the maturation process.

Maturation and quasiequivalence in the covalently linked capsid of phage HK97