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. 2017 May 23;8:15411. doi: 10.1038/ncomms15411

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Copyright © 2017, The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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(a) The previously determined structure of DENV2 sE WT in complex with EDE2 A11 Fab (PDB code 4UTB). The molecular two-fold axis is shown as a light-brown central rod, and the cysteines are displayed as green spheres. The heavy and light chains of Fab A11 are coloured in green and light grey, respectively. sE proteins are colour-coded by domains: domain I–red, domain II–yellow and domain III–blue. (b,c) Structures determined here of DENV2 sE A259C mutant in complex with anti-EDE2 A11 Fab (b) and DENV2 sE L107/A313C mutant in complex with anti-EDE2 A11 Fab (c). The constant domains of the two Fab A11 in DENV2 sE A259C complex were disordered in the final structure and thereby are shown in transparent ribbons. Lower b,c: zoom views of the engineered disulfides are shown respectively for DENV2 sE A259C in complex with anti-EDE2 A11 Fab and DENV2 sE L107/A313C in complex with anti-EDE2 A11 Fab.