Fig. 2: ACNDV Cp at pH 7.5 and pH 5.5 have the same protein fold. | Nature Communications

Fig. 2: ACNDV Cp at pH 7.5 and pH 5.5 have the same protein fold.

From: Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style

Fig. 2

a, d Cryo-EM micrograph of ACNDV capsids at pH 7.5 and pH 5.5 showing icosahedral T = 3 particles. b, e Cryo-EM density maps of the ACNDV capsid at pH 7.5, (resolution of 3.7 Å) plotted at a contour level of 4σ and of the ACNDV capsid at pH 5.5 (resolution of 3.9 Å plotted at a contour level of 3σ. c, f Whole capsid structures where chain A of the asymmetric unit is colored in green, chain B in orange and chain C in blue. The white shapes indicate the symmetry axes in the T = 3 particle. Chains within the black rhombus are schematically shown in panel g. g Schematic representation of chains showing their organization in T = 3 symmetry capsids. h Asymmetric unit of the ACNDV capsid at pH 7.5. The spike residues 66–74 and the N-terminal residue were omitted in the structure due to a lack of well-resolved map density. A dotted line is displayed to show the connectivity of the protein at the spikes. i Superposition (matchmaker in ChimeraX80) of the asymmetric units of the ACNDV capsid at pH 7.5 (blue) and pH 5.5 (yellow). The positions of the α + helices are marked in red.

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