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. 2005;437(7059):764–769. doi: 10.1038/nature03956

Figure 1. Crystal structure of the E16 Fab in complex with DIII of West Nile virus envelope glycoprotein.

Figure 1

a, Ribbon diagram of the complex, with DIII depicted in dark blue, the antibody heavy chain in green and the light chain in cyan. b, Molecular surface representation of the E16–DIII interface highlighting E16 VH (green) and VL (cyan) contact residues (left), as well as DIII contact residues (blue) and the residues defined by yeast surface display (magenta) (right). c, Flow cytometry of yeast cells expressing wild-type or mutant versions of West Nile virus DIII. d, Detailed interactions of DIII residues Ser 306 and Lys 307 with E16, with interfacial waters (red) evident in the composite electron density omit map. e, Interactions of Thr 330 and Thr 332 at the E16 interface.