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. 2012 May 10;8(5):e1002502. doi: 10.1371/journal.pcbi.1002502

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Larrson et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Van der Waals surfaces of the capsid shell after 1 viewed along one of the 5-fold symmetry axes. Top row (A, B) shows and bottom row (C, D) shows . Right column (B, D) shows the interior structure when the 15 frontmost proteins has been removed. Each capsid inscribed in an icosahedron with 22 nm between opposing vertices. The N-terminal domains are represented as ribbons. Colors according to the RMSd from the crystal structure. The color scale goes from blue (0.0 nm) through cyan, green, lime-green, yellow and red (). Location of symmetry axes marked for one icosahedral face in (A). The outline of the proteins in one trimer traced in (C).

Inline graphic — Van der Waals surfaces of the capsid shell after 1 viewed along one of the 5-fold symmetry axes. Top row (A, B) shows and bottom row (C, D) shows . Right column (B, D) shows the interior structure when the 15 frontmost proteins has been removed. Each capsid inscribed in an icosahedron with 22 nm between opposing vertices. The N-terminal domains are represented as ribbons. Colors according to the RMSd from the crystal structure. The color scale goes from blue (0.0 nm) through cyan, green, lime-green, yellow and red (). Location of symmetry axes marked for one icosahedral face in (A). The outline of the proteins in one trimer traced in (C).