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. 2001 Mar;75(6):2879–2890. doi: 10.1128/JVI.75.6.2879-2890.2001

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Copyright © 2001, American Society for Microbiology

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FIG. 1 — Cryo-EM of KSHV capsids. (A) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis with Coomassie blue staining of purified capsids. The four bands marked with asterisks represent, from the top, the major capsid protein (ORF25), the triplex α-subunit (ORF62), the triplex β-subunit (ORF26), and the small basic capsid protein (ORF65). The identification of these proteins is described in the accompanying paper (26). (B) Cryo-electron micrograph showing a field containing several empty capsids (A-capsids). (C) Distribution over the icosahedral asymmetric unit of the orientations of imaged particles (2). , twofold axis; ▴, threefold axis; , fivefold axis.

Inline graphic — Cryo-EM of KSHV capsids. (A) Sodium dodecyl sulfate-polyacrylamide gel electrophoresis with Coomassie blue staining of purified capsids. The four bands marked with asterisks represent, from the top, the major capsid protein (ORF25), the triplex α-subunit (ORF62), the triplex β-subunit (ORF26), and the small basic capsid protein (ORF65). The identification of these proteins is described in the accompanying paper (26). (B) Cryo-electron micrograph showing a field containing several empty capsids (A-capsids). (C) Distribution over the icosahedral asymmetric unit of the orientations of imaged particles (2). , twofold axis; ▴, threefold axis; , fivefold axis.