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Open data
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Basic information
| Entry | Database: PDB / ID: 7efc | ||||||
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| Title | 1.70 A cryo-EM structure of streptavidin | ||||||
Components | Streptavidin | ||||||
Keywords | CYTOSOLIC PROTEIN / STREPTAVIDIN | ||||||
| Function / homology | Function and homology information | ||||||
| Biological species | Streptomyces avidinii (bacteria) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 1.7 Å | ||||||
Authors | Hiraizumi, M. / Yamashita, K. / Nishizawa, T. / Kotecha, A. / Nureki, O. | ||||||
Citation | Journal: To Be PublishedTitle: 1.70 A cryo-EM structure of streptavidin using all frames (corresponding to 70 e/A^2 total dose) Authors: Hiraizumi, M. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7efc.cif.gz | 42.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7efc.ent.gz | 24.5 KB | Display | PDB format |
| PDBx/mmJSON format | 7efc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7efc_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 7efc_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 7efc_validation.xml.gz | 21.7 KB | Display | |
| Data in CIF | 7efc_validation.cif.gz | 30.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ef/7efc ftp://data.pdbj.org/pub/pdb/validation_reports/ef/7efc | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 31083MC ![]() 7efdC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 3 | ![]()
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| Symmetry | Point symmetry: (Schoenflies symbol: D2 (2x2 fold dihedral)) | ||||||||||||||||||||
| Noncrystallographic symmetry (NCS) | NCS oper:
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Components
| #1: Protein | Mass: 18849.672 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Streptomyces avidinii (bacteria) / References: UniProt: P22629 |
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| #2: Chemical | ChemComp-BTN / |
| #3: Water | ChemComp-HOH / |
| Has ligand of interest | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Streptavidin / Type: COMPLEX / Entity ID: #1 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Streptomyces avidinii (bacteria) |
| Buffer solution | pH: 7.2 |
| Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: UltrAuFoil R1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 70 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 4053 |
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Processing
| Software | Name: REFMAC / Version: 5.8.0272 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: D2 (2x2 fold dihedral) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 1.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 153976 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Space: RECIPROCAL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | 3D fitting-ID: 1 / Source name: PDB / Type: experimental model
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| Refinement | Resolution: 1.7→76.255 Å / Cor.coef. Fo:Fc: 0.89 / WRfactor Rwork: 0.356 / SU B: 4.072 / SU ML: 0.104 / Average fsc overall: 0.6041 / Average fsc work: 0.6041 / ESU R: 0.049 Details: Hydrogens have been added in their riding positions
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| Solvent computation | Solvent model: BABINET MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 44.597 Å2
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| Refine LS restraints |
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Streptomyces avidinii (bacteria)
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