+Open data
-Basic information
Entry | Database: PDB / ID: 9d9x | |||||||||||||||||||||||||||
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Title | Mycobacteriophage Bxb1 Capsid - Composite map and model | |||||||||||||||||||||||||||
Components | Major capsid protein | |||||||||||||||||||||||||||
Keywords | VIRAL PROTEIN / Bacteriophage / capsid / VIRUS | |||||||||||||||||||||||||||
Function / homology | Phage capsid / Phage capsid family / Major capsid protein Function and homology information | |||||||||||||||||||||||||||
Biological species | Mycobacterium phage Bxb1 (virus) | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | |||||||||||||||||||||||||||
Authors | Freeman, K.G. | |||||||||||||||||||||||||||
Funding support | United States, Taiwan, 8items
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Citation | Journal: To Be Published Title: Structure and infection dynamics of mycobacteriophage Bxb1 Authors: Freeman, K.G. / Mondal, S. / Macale, L.S. / Podgorski, J. / White, S.J. / Silva, B. / Ortiz, V. / Huet, A. / Narsico, J.T. / Ho, M.C. / Jacobs-Sera, D. / Lowary, T.L. / Conway, J.F. / Park, D. / Hatfull, G.F. | |||||||||||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 9d9x.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb9d9x.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 9d9x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 9d9x_validation.pdf.gz | 877.9 KB | Display | wwPDB validaton report |
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Full document | 9d9x_full_validation.pdf.gz | 880.1 KB | Display | |
Data in XML | 9d9x_validation.xml.gz | 101.1 KB | Display | |
Data in CIF | 9d9x_validation.cif.gz | 156.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d9/9d9x ftp://data.pdbj.org/pub/pdb/validation_reports/d9/9d9x | HTTPS FTP |
-Related structure data
Related structure data | 46685MC 9d93C 9d94C 9d9lC 9d9wC C: citing same article (ref.) M: map data used to model this data |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 41875.461 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Source: (natural) Mycobacterium phage Bxb1 (virus) / References: UniProt: Q9B0A7 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Mycobacterium phage Bxb1 / Type: VIRUS Details: Portal and connector complex of Bxb1, containing five protein subunit types. This is a composite map, and related entries for consensus and locally refined maps are noted. Entity ID: all / Source: NATURAL | |||||||||||||||||||||||||
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Molecular weight |
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Source (natural) | Organism: Mycobacterium phage Bxb1 (virus) / Strain: Mycobacterium phage Bxb1 | |||||||||||||||||||||||||
Details of virus | Empty: NO / Enveloped: NO / Isolate: SPECIES / Type: VIRION | |||||||||||||||||||||||||
Natural host | Organism: Mycolicibacterium smegmatis MC2 155 | |||||||||||||||||||||||||
Buffer solution | pH: 7.5 | |||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 10 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 283 K |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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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: 2500 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3 Å / Resolution method: OTHER / Num. of particles: 23927 / Symmetry type: POINT |