+Open data
-Basic information
Entry | Database: PDB / ID: 8qi0 | |||||||||
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Title | 340A Vipp1 H1-6 helical tubes | |||||||||
Components | Membrane-associated protein Vipp1 | |||||||||
Keywords | LIPID BINDING PROTEIN / membrane remodeling / membrane tubulation | |||||||||
Function / homology | PspA/IM30 / PspA/IM30 family / plasma membrane / Membrane-associated protein Vipp1 Function and homology information | |||||||||
Biological species | Synechocystis sp. PCC 6803 (bacteria) | |||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 6.7 Å | |||||||||
Authors | Junglas, B. / Sachse, C. | |||||||||
Funding support | Germany, 2items
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Citation | Journal: To Be Published Title: Structural basis for Vipp1 membrane binding: From rings and rods to carpets Authors: Junglas, B. / Kartte, D. / Ritter, I. / Schneider, D. / Sachse, C. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8qi0.cif.gz | 36.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8qi0.ent.gz | 20.3 KB | Display | PDB format |
PDBx/mmJSON format | 8qi0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8qi0_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 8qi0_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 8qi0_validation.xml.gz | 24.9 KB | Display | |
Data in CIF | 8qi0_validation.cif.gz | 34.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qi/8qi0 ftp://data.pdbj.org/pub/pdb/validation_reports/qi/8qi0 | HTTPS FTP |
-Related structure data
Related structure data | 18429MC 8qfvC 8qhvC 8qhwC 8qhxC 8qhyC 8qhzC 8qi1C 8qi2C 8qi3C 8qi4C 8qi5C 8qi6C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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-Components
#1: Protein | Mass: 21060.562 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Synechocystis sp. PCC 6803 (bacteria) / Gene: vipp1, sll0617 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q55707 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction |
-Sample preparation
Component | Name: Vipp1 H1-6 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Synechocystis sp. PCC 6803 (bacteria) |
Source (recombinant) | Organism: Escherichia coli BL21(DE3) (bacteria) / Strain: C41 |
Buffer solution | pH: 8 |
Specimen | Embedding applied: YES / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
EM embedding | Material: vitreous ice |
Vitrification | Cryogen name: ETHANE |
-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: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 48 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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Helical symmerty | Angular rotation/subunit: -21.7 ° / Axial rise/subunit: 7.48 Å / Axial symmetry: C4 |
3D reconstruction | Resolution: 6.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 48681 / Symmetry type: HELICAL |