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Yorodumi- EMDB-16956: Cryo-EM reconstruction of VP4 assembly from SA11 Rotavirus Non-Tr... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-16956 | |||||||||
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Title | Cryo-EM reconstruction of VP4 assembly from SA11 Rotavirus Non-Tripsinized Triple Layered Particle | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Rotavirus / dsRNA virus / VIRUS | |||||||||
Function / homology | Function and homology information host cell rough endoplasmic reticulum / permeabilization of host organelle membrane involved in viral entry into host cell / host cytoskeleton / viral outer capsid / host cell endoplasmic reticulum-Golgi intermediate compartment / virion attachment to host cell / host cell plasma membrane / membrane Similarity search - Function | |||||||||
Biological species | Rotavirus / Rotavirus A | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.4 Å | |||||||||
Authors | Asensio-Cob D / Perez-Mata C / Gomez-Blanco J / Vargas J / Rodriguez JM / Luque D | |||||||||
Funding support | Spain, 1 items
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Citation | Journal: To Be Published Title: Structural basis of rotavirus spike proteolytic activation Authors: Asensio-Cob D / Perez-Mata C / Gomez-Blanco J / Vargas J / Rodriguez JM / Luque D | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_16956.map.gz | 27.1 MB | EMDB map data format | |
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Header (meta data) | emd-16956-v30.xml emd-16956.xml | 16.3 KB 16.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_16956_fsc.xml | 9.1 KB | Display | FSC data file |
Images | emd_16956.png | 66.9 KB | ||
Filedesc metadata | emd-16956.cif.gz | 6 KB | ||
Others | emd_16956_half_map_1.map.gz emd_16956_half_map_2.map.gz | 23.4 MB 23.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16956 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16956 | HTTPS FTP |
-Validation report
Summary document | emd_16956_validation.pdf.gz | 639.1 KB | Display | EMDB validaton report |
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Full document | emd_16956_full_validation.pdf.gz | 638.7 KB | Display | |
Data in XML | emd_16956_validation.xml.gz | 12.8 KB | Display | |
Data in CIF | emd_16956_validation.cif.gz | 17.9 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16956 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16956 | HTTPS FTP |
-Related structure data
Related structure data | 8oleMC 8olbC 8olcC 8qtzC 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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-Map
File | Download / File: emd_16956.map.gz / Format: CCP4 / Size: 30.5 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: 1.34 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_16956_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_16956_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Rotavirus A
Entire | Name: Rotavirus A |
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Components |
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-Supramolecule #1: Rotavirus A
Supramolecule | Name: Rotavirus A / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Rotavirus SA11 Non-tripsinized spike / NCBI-ID: 28875 / Sci species name: Rotavirus A / Sci species strain: SA11 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: Chlorocebus aethiops (grivet) |
Molecular weight | Theoretical: 92 MDa |
Virus shell | Shell ID: 1 / Name: TLP / Diameter: 700.0 Å |
-Macromolecule #1: Outer capsid protein VP4
Macromolecule | Name: Outer capsid protein VP4 / type: protein_or_peptide / ID: 1 / Details: Outer capsid protein VP4 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Rotavirus |
Molecular weight | Theoretical: 86.749891 KDa |
Recombinant expression | Organism: Chlorocebus aethiops (grivet) |
Sequence | String: MASLIYRQLL TNSYTVDLSD EIQEIGSTKS QNVTINPGPF AQTGYAPVNW GPGEINDSTT VEPLLDGPYQ PTTFNPPVDY WMLLAPTTP GVIVEGTNNT DRWLATILIE PNVQSENRTY TIFGIQEQLT VSNTSQDQWK FIDVVKTTAN GSIGQYGSLL S SPKLYAVM ...String: MASLIYRQLL TNSYTVDLSD EIQEIGSTKS QNVTINPGPF AQTGYAPVNW GPGEINDSTT VEPLLDGPYQ PTTFNPPVDY WMLLAPTTP GVIVEGTNNT DRWLATILIE PNVQSENRTY TIFGIQEQLT VSNTSQDQWK FIDVVKTTAN GSIGQYGSLL S SPKLYAVM KHNEKLYTYE GQTPNARTGH YSTTNYDSVN MTAFCDFYII PRSEESKCTE YINNGLPPIQ NTRNVVPLSL TA RDVIHYR AQANEDIVIS KTSLWKEMQY NRDITIRFKF ANTIIKSGGL GYKWSEISFK PANYQYTYTR DGEEVTAHTT CSV NGVNDF SFNGGSLPTD FVVSKFEVIK ENSYVYIDYW DDSQAFRNVV YVRSLAANLN SVMCTGGSYN FSLPVGQWPV LTGG AVSLH SAGVTLSTQF TDFVSLNSLR FRFRLAVEEP HFKLTRTRLD RLYGLPAADP NNGKEYYEIA GRFSLISLVP SNDDY QTPI ANSVTVRQDL ERQLGELREE FNALSQEIAM SQLIDLALLP LDMFSMFSGI KSTIDAAKSM ATNVMKKFKK SGLANS VST LTDSLSDAAS SISRGSSIRS IGSSASAWTD VSTQITDISS SVSSVSTQTS TISRRLRLKE MATQTEGMNF DDISAAV LK TKIDKSTQIS PNTIPDIVTE ASEKFIPNRA YRVINNDDVF EAGIDGKFFA YKVDTFEEIP FDVQKFADLV TDSPVISA I IDFKTLKNLN DNYGITKQQA FNLLRSDPRV LREFINQDNP IIRNRIEQLI MQCRL UniProtKB: Outer capsid protein VP4 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Grid | Model: Quantifoil R2/2 / Material: COPPER/RHODIUM / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 10 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 295 K / Instrument: LEICA EM GP |
Details | Rotavirus SA11 Non-tripsinized spike |
-Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Number real images: 1465 / Average electron dose: 42.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.75 µm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |