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Yorodumi- EMDB-28627: Cryo-EM structure of Coxsackievirus A10 (empty) embedded in cryst... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-28627 | |||||||||
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Title | Cryo-EM structure of Coxsackievirus A10 (empty) embedded in crystalline ice | |||||||||
Map data | The EM map of Coxsackie A10 virus like particle (empty) embedded in crystalline ice frozen at -140 celsius degree. The resolution of EM map is 3.1 angstrom. | |||||||||
Sample |
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Keywords | Coxsackie A10 VLP / Crystalline ice / Crystal ice / VIRUS LIKE PARTICLE | |||||||||
Function / homology | Function and homology information symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase ...symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / metal ion binding Similarity search - Function | |||||||||
Biological species | Coxsackievirus A10 | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Shi H / Wu C / Zhang X | |||||||||
Funding support | China, 1 items
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Citation | Journal: Structure / Year: 2023 Title: Addressing compressive deformation of proteins embedded in crystalline ice. Authors: Huigang Shi / Chunling Wu / Xinzheng Zhang / Abstract: For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. ...For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_28627.map.gz | 285.9 MB | EMDB map data format | |
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Header (meta data) | emd-28627-v30.xml emd-28627.xml | 39.5 KB 39.5 KB | Display Display | EMDB header |
Images | emd_28627.png | 44 KB | ||
Masks | emd_28627_msk_1.map | 421.9 MB | Mask map | |
Filedesc metadata | emd-28627.cif.gz | 4.7 KB | ||
Others | emd_28627_additional_1.map.gz emd_28627_additional_10.map.gz emd_28627_additional_11.map.gz emd_28627_additional_12.map.gz emd_28627_additional_2.map.gz emd_28627_additional_3.map.gz emd_28627_additional_4.map.gz emd_28627_additional_5.map.gz emd_28627_additional_6.map.gz emd_28627_additional_7.map.gz emd_28627_additional_8.map.gz emd_28627_additional_9.map.gz emd_28627_half_map_1.map.gz emd_28627_half_map_2.map.gz | 337.7 MB 337.2 MB 337.6 MB 337.3 MB 395 MB 338.1 MB 387.2 MB 385.8 MB 337.3 MB 395.6 MB 337.8 MB 337.4 MB 337.1 MB 337.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-28627 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28627 | HTTPS FTP |
-Validation report
Summary document | emd_28627_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
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Full document | emd_28627_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | emd_28627_validation.xml.gz | 18.7 KB | Display | |
Data in CIF | emd_28627_validation.cif.gz | 21.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28627 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28627 | HTTPS FTP |
-Related structure data
Related structure data | 8bqnMC 8ew0C 8ew2C 8f49C 8f7yC 8hhsC 8hi2C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_28627.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | The EM map of Coxsackie A10 virus like particle (empty) embedded in crystalline ice frozen at -140 celsius degree. The resolution of EM map is 3.1 angstrom. | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.836 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
+Mask #1
+Additional map: The half map of Coxsackie A10 virus like...
+Additional map: The half map of Coxsackie A10 virus like...
+Additional map: The half map of Coxsackie A10 virus like...
+Additional map: The half map of Coxsackie A10 virus like...
+Additional map: The EM map of Coxsackie A10 virus like...
+Additional map: The half map of Coxsackie A10 virus like...
+Additional map: The EM map of Coxsackie A10 virus like...
+Additional map: The EM map of Coxsackie A10 virus like...
+Additional map: The half map of Coxsackie A10 virus like...
+Additional map: The EM map of Coxsackie A10 virus like...
+Additional map: The half map of Coxsackie A10 virus like...
+Additional map: The half map of Coxsackie A10 virus like...
+Half map: The half map of Coxsackie A10 virus like...
+Half map: The half map of Coxsackie A10 virus like...
-Sample components
-Entire : Coxsackievirus A10
Entire | Name: Coxsackievirus A10 |
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Components |
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-Supramolecule #1: Coxsackievirus A10
Supramolecule | Name: Coxsackievirus A10 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 42769 / Sci species name: Coxsackievirus A10 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: SUBSPECIES / Virus enveloped: No / Virus empty: Yes |
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-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 6.8 / Details: PBS, Ph 6.8 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 298 K / Instrument: LEICA PLUNGER |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |