Fig. 5
From: Sub-2 Å Ewald curvature corrected structure of an AAV2 capsid variant

Comparison of AAV2WT and AAV2L336C. a The density map with the modeled residues for the DE-loop for AAV2WT and AAV2L336C. The wild-type L336 and substituted C336 residues are shown. The AAV2WT has been the highest resolution density map for AAV2 published to date, at 3 Å. The amino-acid residues are shown as stick representation and colored according to atom type: C = yellow, O = red, N = blue, H = white, S = green inside a black mesh density map. b Superposed pentamer models of AAV2WT (blue) and AAV2L336C (yellow). Lower panel show close-up views of the fivefold region as side view and top view perspectives. Side-chain atoms for individual residues of interest are shown