1. The Crystal Structure of the Human Hepatitis B Virus Capsid
S.A Wynne, R.A Crowther, A.G.W Leslie 
Molecular Cell 
Volume 3, Issue 6, Pages (June 1999)
DOI: /S (01)

2. Figure 1 The Experimental Electron Density Map
Stereo view of a portion of the experimental electron density map following phase extension to 3.3 Å, showing parts of the α-helical hairpins in subunits C and D, with the final refined model superimposed.
Molecular Cell 1999 3, DOI: ( /S (01) )

3. Figure 5 Packing of Dimers in the T = 4 Capsid
(a) A schematic representation of the arrangement of the four independent subunits in the T = 4 capsid, showing one icosahedral face. The subunit nomenclature follows Zlotnick et al The positions of the four-helix bundles are shown by black circles.
(b) Stereo view of the packing of the dimers in the T = 4 capsid in the region of a quasi three-fold axis. Subunits A, B, C, and D are shown in green, yellow, red, and blue as in Böttcher et al The positions of the icosahedral five-fold (5), three-fold (3), quasi three-fold (q3), and two-fold (2) axes are shown.
(c) The capsid viewed down an icosahedral three-fold axis.
Molecular Cell 1999 3, DOI: ( /S (01) )

4. Figure 2 Structure and Sequence of the HBV Capsid Monomer
A schematic representation of the fold of the HBV capsid protein monomer derived from the crystal structure (a) and from electron cryomicroscopy (b). The cryo EM fold is taken directly from Böttcher et al. 1997, but the hand has been inverted to match that of the X-ray structure. The dimer interface is nearest the viewer. (c) The amino acid sequence of the CW variant of HBV capsid, truncated at amino acid 149 for this study (indicated by Δ). The positions of the helices are shown. The 94 full-length human HBV capsid sequences in the SWISS-PROT and TrEMBL databases (Bairoch and Apweiler 1998) were aligned using CLUSTALW. Fully conserved residues (identical in all 94 sequences) are marked (*).
Molecular Cell 1999 3, DOI: ( /S (01) )

5. Figure 3 Hydrophobic Core of the Monomer
A stereo view of the monomer showing the hydrophobic core, formed by residues Tyr-6, Phe-9, Leu-15, Leu-16, Phe-18, Leu-19, Phe-23, Phe-24, Trp-102, Phe-103, Phe-110, Val-115, Tyr-118, Leu-119, Phe-122, Trp-125, and Leu-140, some of which are labeled. The dimer interface is away from the viewer.
Molecular Cell 1999 3, DOI: ( /S (01) )

6. Figure 4 The HBV Capsid Dimer
Two orthogonal views of the HBV capsid protein dimer (subunits C and D) viewed normal to the local two-fold axis and along the two-fold axis from the outside of the capsid. Cys-61, which forms a disulfide bridge between the two monomers, is shown in green, and Cys-48, which does not form disulfides, in yellow. The C-terminal regions provide most of the interdimer interactions that build the capsid.
Molecular Cell 1999 3, DOI: ( /S (01) )

7. Figure 6 Dimer–Dimer Interactions in the Capsid
A stereo view from outside the capsid of the interactions between adjacent subunits around (a) the five-fold (A subunits) and (b) the two-fold (quasi six-fold) axes (B, C, and D subunits). In each case, the polypeptide chain is color ramped from blue (aa 115) to red (aa 142). Residues that play an important role in intersubunit contacts or in stabilizing the conformation of the proline-rich loop (aa 128–136) are indicated. For clarity, the side chains of residues 115–121 have been omitted.
Molecular Cell 1999 3, DOI: ( /S (01) )

8. Figure 7 The Major Immunodominant Region
Stereo view of the tip of the α-helical hairpin of subunit C, with the dimer interface away from the viewer. The major immunodominant region has been mapped to residues 78–83. Foreign sequences of up to 46 aa can be inserted between residues 78 and 79 without preventing capsid assembly.
Molecular Cell 1999 3, DOI: ( /S (01) )