Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins
Fig 5
Additional internal components of the FAdV-C4 capsid.
(a) FAdV-C4 map, as viewed from inside of the capsid. Left: only the density corresponding to the traced proteins is shown. The two-fold (oval), three-fold (triangle) and five-fold (pentagon) symmetry axes, the four hexons in one AU (H1-H4), and the facet (dashed triangle) are indicated for reference. Right: remnant densities (RD) are coloured in red. (b) Remnant map components colour-coded as RD1-4. Right: a zoom showing only the colour-coded RDs. RDs considered too small to be analysed are left in grey. Densities correspond to the unsharpened map contoured at 1.5 σ. Hexagon contours indicate hexon positions.