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Yorodumi- EMDB-4634: Localized reconstruction of archaeal virus SH1 vertex calculated ... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-4634 | |||||||||||||||
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| Title | Localized reconstruction of archaeal virus SH1 vertex calculated without symmetry | |||||||||||||||
Map data | Localized asymmetric reconstruction of archaeal virus SH1 vertex | |||||||||||||||
Sample |
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| Biological species | Haloarcula hispanica virus SH1 | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 7.3 Å | |||||||||||||||
Authors | De Colibus L / Ilca SL / Stuart DIS / Huiskonen JT | |||||||||||||||
| Funding support | United Kingdom, Finland, 4 items
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Citation | Journal: Nat Commun / Year: 2019Title: Assembly of complex viruses exemplified by a halophilic euryarchaeal virus. Authors: Luigi De Colibus / Elina Roine / Thomas S Walter / Serban L Ilca / Xiangxi Wang / Nan Wang / Alan M Roseman / Dennis Bamford / Juha T Huiskonen / David I Stuart / ![]() Abstract: Many of the largest known viruses belong to the PRD1-adeno structural lineage characterised by conserved pseudo-hexameric capsomers composed of three copies of a single major capsid protein (MCP). ...Many of the largest known viruses belong to the PRD1-adeno structural lineage characterised by conserved pseudo-hexameric capsomers composed of three copies of a single major capsid protein (MCP). Here, by high-resolution cryo-EM analysis, we show that a class of archaeal viruses possess hetero-hexameric MCPs which mimic the PRD1-adeno lineage trimer. These hetero-hexamers are built from heterodimers and utilise a jigsaw-puzzle system of pegs and holes, and underlying minor capsid proteins, to assemble the capsid laterally from the 5-fold vertices. At these vertices proteins engage inwards with the internal membrane vesicle whilst 2-fold symmetric horn-like structures protrude outwards. The horns are assembled from repeated globular domains attached to a central spine, presumably facilitating multimeric attachment to the cell receptor. Such viruses may represent precursors of the main PRD1-adeno lineage, similarly engaging cell-receptors via 5-fold spikes and using minor proteins to define particle size. | |||||||||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_4634.map.gz | 92.7 MB | EMDB map data format | |
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| Header (meta data) | emd-4634-v30.xml emd-4634.xml | 12.4 KB 12.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_4634_fsc.xml | 10.8 KB | Display | FSC data file |
| Images | emd_4634.png | 161.7 KB | ||
| Masks | emd_4634_msk_1.map | 103 MB | Mask map | |
| Others | emd_4634_additional.map.gz emd_4634_additional_1.map.gz | 58 MB 58 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-4634 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4634 | HTTPS FTP |
-Validation report
| Summary document | emd_4634_validation.pdf.gz | 319.6 KB | Display | EMDB validaton report |
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| Full document | emd_4634_full_validation.pdf.gz | 318.7 KB | Display | |
| Data in XML | emd_4634_validation.xml.gz | 11.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4634 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4634 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_4634.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Localized asymmetric reconstruction of archaeal virus SH1 vertex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
| File | emd_4634_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Additional map: Map filtered to local resolution
| File | emd_4634_additional.map | ||||||||||||
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| Annotation | Map filtered to local resolution | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Additional map: Map filtered to local resolution
| File | emd_4634_additional_1.map | ||||||||||||
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| Annotation | Map filtered to local resolution | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Haloarcula hispanica virus SH1
| Entire | Name: Haloarcula hispanica virus SH1 |
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| Components |
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-Supramolecule #1: Haloarcula hispanica virus SH1
| Supramolecule | Name: Haloarcula hispanica virus SH1 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 326574 / Sci species name: Haloarcula hispanica virus SH1 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: Yes / Virus empty: No |
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| Virus shell | Shell ID: 1 / Name: Capsid / Diameter: 1000.0 Å / T number (triangulation number): 28 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 15 mg/mL |
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| Buffer | pH: 7.2 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI POLARA 300 |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 1.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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About Yorodumi


Haloarcula hispanica virus SH1
Authors
United Kingdom,
Finland, 4 items
Citation
UCSF Chimera








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Processing

