+Open data
-Basic information
Entry | Database: PDB / ID: 8ean | ||||||
---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of in-situ tailspike in bacteriophage P22 | ||||||
Components | Tail spike protein | ||||||
Keywords | VIRAL PROTEIN / Bacteriophage P22 | ||||||
Function / homology | Function and homology information endo-1,3-alpha-L-rhamnosidase activity / symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide / virus tail, fiber / symbiont entry into host cell via disruption of host cell envelope / symbiont entry into host / Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / adhesion receptor-mediated virion attachment to host cell / virion attachment to host cell Similarity search - Function | ||||||
Biological species | Salmonella phage P22 (virus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||
Authors | Wang, C. / Liu, J. / Molineux, I.J. | ||||||
Funding support | United States, 1items
| ||||||
Citation | Journal: To Be Published Title: In-situ structure of tail machine reveals mechanistic insights into P22 assembly. Authors: Wang, C. / Liu, J. / Molineux, I.J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 8ean.cif.gz | 330.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb8ean.ent.gz | 270.1 KB | Display | PDB format |
PDBx/mmJSON format | 8ean.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8ean_validation.pdf.gz | 744 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 8ean_full_validation.pdf.gz | 787.1 KB | Display | |
Data in XML | 8ean_validation.xml.gz | 62.1 KB | Display | |
Data in CIF | 8ean_validation.cif.gz | 97.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ea/8ean ftp://data.pdbj.org/pub/pdb/validation_reports/ea/8ean | HTTPS FTP |
-Related structure data
Related structure data | 27791MC 8eaoC M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
#1: Protein | Mass: 71361.875 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Salmonella phage P22 (virus) References: UniProt: P12528, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Cryo-EM structure of in-situ tailspike from bacteriophage P22 Type: COMPLEX / Entity ID: all / Source: NATURAL |
---|---|
Source (natural) | Organism: Salmonella phage P22 (virus) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1200 nm / Nominal defocus min: 600 nm |
Image recording | Electron dose: 30 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 195900 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
|