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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-30122 | |||||||||
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| Title | Asymmetric reconstrcution of HSV2 C capsid | |||||||||
Map data | ||||||||||
Sample |
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| Biological species | ![]() Human alphaherpesvirus 2 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 9.0 Å | |||||||||
Authors | Wang XX / Wang N | |||||||||
Citation | Journal: Protein Cell / Year: 2020Title: Structures of the portal vertex reveal essential protein-protein interactions for Herpesvirus assembly and maturation. Authors: Nan Wang / Wenyuan Chen / Ling Zhu / Dongjie Zhu / Rui Feng / Jialing Wang / Bin Zhu / Xinzheng Zhang / Xiaoqing Chen / Xianjie Liu / Runbin Yan / Dongyao Ni / Grace Guoying Zhou / Hongrong ...Authors: Nan Wang / Wenyuan Chen / Ling Zhu / Dongjie Zhu / Rui Feng / Jialing Wang / Bin Zhu / Xinzheng Zhang / Xiaoqing Chen / Xianjie Liu / Runbin Yan / Dongyao Ni / Grace Guoying Zhou / Hongrong Liu / Zihe Rao / Xiangxi Wang / ![]() | |||||||||
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Structure visualization
| Movie |
Movie viewer |
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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_30122.map.gz | 220.8 MB | EMDB map data format | |
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| Header (meta data) | emd-30122-v30.xml emd-30122.xml | 7.8 KB 7.8 KB | Display Display | EMDB header |
| Images | emd_30122.png | 84.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-30122 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-30122 | HTTPS FTP |
-Validation report
| Summary document | emd_30122_validation.pdf.gz | 426.4 KB | Display | EMDB validaton report |
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| Full document | emd_30122_full_validation.pdf.gz | 426 KB | Display | |
| Data in XML | emd_30122_validation.xml.gz | 8.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30122 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-30122 | 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_30122.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 2.76 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Human alphaherpesvirus 2
| Entire | Name: ![]() Human alphaherpesvirus 2 |
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| Components |
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-Supramolecule #1: Human alphaherpesvirus 2
| Supramolecule | Name: Human alphaherpesvirus 2 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 10310 / Sci species name: Human alphaherpesvirus 2 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: Yes / Virus empty: No |
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| Host (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 30.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DARK FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 9.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 71956 |
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| Initial angle assignment | Type: RANDOM ASSIGNMENT |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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Human alphaherpesvirus 2
Authors
Citation
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Y (Row.)
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Homo sapiens (human)
