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( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). <t>Unmodeled</t> <t>N-terminal</t> extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.
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( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). <t>Unmodeled</t> <t>N-terminal</t> extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.
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( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). <t>Unmodeled</t> <t>N-terminal</t> extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.
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Image Search Results


( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). Unmodeled N-terminal extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.

Journal: bioRxiv

Article Title: Conserved assembly architecture of the essential herpesvirus packaging accessory factor

doi: 10.64898/2026.01.22.701024

Figure Lengend Snippet: ( a ) At lower contour levels the 3-mer reconstruction shows the presence of a weakly associated fourth protomer. Map color by local resolution, scale bar has the same blue-red color scale as in , with lower resolutions beyond 4.55 Å shown in dark red. ( b ) Details of the cross section from the 3-mer reconstruction highlights resolvable features at the interface where a fourth protomer could bind. Model for a fourth protomer is shown in dark blue. ( c ) Schematic of the UL52 sequence showing surface regions that could not be modeled (grey). Insets show the sequence of negatively charged disordered loops that extend from the top of the incomplete ring. ( d ) Model showing two major regions of UL52 surface remodeling relative to ORF68 (yellow and orange). Unmodeled N-terminal extension (light blue) and long disordered top loop (dark blue) are represented as dashed lines.

Article Snippet: The coding region of UL52 was subcloned from a pcDNA4/TO-2xStrep vector (Addgene #162628) into a pHEK293 UltraExpression I vector (Clontech) that encodes an N-terminal Twin-Strep tag and HRV 3C protease cleavage site (pUE1-TSP) to generate pUE1-TSP-UL52.

Techniques: Sequencing

(a) Cryo-EM density map (transparent, moderate contour level) and model (cartoon, colored as in ) of the UL32 tripentamer interface helix and additional stabilizing density modeled as P5-S11 of the N-terminal extension. ( b ) UL32 tripentamer interface helix (green) and corresponding helices from UL52 (blue) and ORF68 (grey). ( c ) Schematic of transient complementation assay. ( d ) Model of tripentamer interface highlighting charge swap mutant R440E. Model displayed colored as in . ( e ) Representative western blot for expression of UL32 WT and mutants in transient complementation assay. ( f ) Graph of total viral yield of UL32 mutants in a transient complementation assay from three independent biological replicates.

Journal: bioRxiv

Article Title: Conserved assembly architecture of the essential herpesvirus packaging accessory factor

doi: 10.64898/2026.01.22.701024

Figure Lengend Snippet: (a) Cryo-EM density map (transparent, moderate contour level) and model (cartoon, colored as in ) of the UL32 tripentamer interface helix and additional stabilizing density modeled as P5-S11 of the N-terminal extension. ( b ) UL32 tripentamer interface helix (green) and corresponding helices from UL52 (blue) and ORF68 (grey). ( c ) Schematic of transient complementation assay. ( d ) Model of tripentamer interface highlighting charge swap mutant R440E. Model displayed colored as in . ( e ) Representative western blot for expression of UL32 WT and mutants in transient complementation assay. ( f ) Graph of total viral yield of UL32 mutants in a transient complementation assay from three independent biological replicates.

Article Snippet: The coding region of UL52 was subcloned from a pcDNA4/TO-2xStrep vector (Addgene #162628) into a pHEK293 UltraExpression I vector (Clontech) that encodes an N-terminal Twin-Strep tag and HRV 3C protease cleavage site (pUE1-TSP) to generate pUE1-TSP-UL52.

Techniques: Cryo-EM Sample Prep, Mutagenesis, Western Blot, Expressing