FIG. 4.

Differences between the empty and full 10HB capsid structures. A) Modeled 10HB residues aa227 to 229 and B) aa709 to 711 shown inside their density maps (black=empty, red=full). Arginine 228 and 710 display a dual conformation exclusively in the full map. C) Modeled residues at the nucleotide binding pocket shown inside their density maps. Extra density for an ordered nucleotide (dAMP) is exclusively in the full map. D) A pentanucleotide built based on density at the 3-fold pocket is shown for the full 10HB capsid structure inside a red mesh density map at a 2 and 1 σ. The location of the 3-fold symmetry axis is indicated. E) Density in the channel at the 5-fold axis for the empty and full 10HB maps is contoured at a 1σ. Residues 188–199 are modeled inside the channel. This figure was generated using UCSF-Chimera (Pettersen et al., 2004).