Fig. 2: The 2D lattice packs tightly and is maintained through disulfide bond formation.
From: Atomic structure of a nudivirus occlusion body protein determined from a 70-year-old crystal sample
a, b Display of the 2D lattice, the reference polyhedrin (blue) and the polyhedrin with which it makes contact are shown in various colours. The two polyhedrin molecules which form the repeating unit are shown without transparency (a) and with fill colour (b). Molecules which do not contact the reference molecule are in grey. Pink arrows and ellipses indicate the 2-fold crystallographic axis. c, d Detailed insets showing the residues which form the asymmetric disulfide bonds. e C139/C207 are partially oxidised cysteine residues positioned near to the unordered C-terminus of neighbouring molecules. f Additional electron density observed at C139/C207. The 2FO – Fc map at 1σ (blue) and FO – Fc at 3σ are shown.
