Conformational Changes in the Hepatitis B Virus Core Protein Are Consistent with a Role for Allostery in Virus Assembly
J. Virol. Packianathan et al. 84: 1607

Supplemental material

Files in this Data Supplement:

  • Supplemental file 1 - Fig. S1 (Density of the E spike as viewed from the F subunit.)
    Fig. S2 (Equivalent view of the F chain.)
    Fig. S3 (Nonreducing SDS-PAGE showing redox state of Cp149-Y132A for assembly studies.)
    Fig. S4 (Comparison of C61S assembly and C61S-reduced Y132A coassembly kinetics over time.)
    Table S1 (Structural comparisons.)
    PDF file, 1.25 MB.
  • Supplemental file 2 - Movie S1 (Extent of conformational change between dimer and capsid conformations by morphing between the two overlays in Fig.2b, using the subdomain color coding of Fig.3 and showing both Cα and surface-shaded views.)
    Zipped QuickTime Movie file, 2.17 MB.