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Open data
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Basic information
Entry | Database: PDB / ID: 9v7j | |||||||||||||||||||||
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Title | Phycobilisome core from Gloeobacter violaceus PCC 7421 | |||||||||||||||||||||
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![]() | PHOTOSYNTHESIS / Phycobilisome | |||||||||||||||||||||
Function / homology | ![]() phycobilisome / plasma membrane-derived thylakoid membrane / photosynthesis / lyase activity Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.85 Å | |||||||||||||||||||||
![]() | Burtseva, A.D. / Baymukhametov, T.N. / Slonimskiy, Y.B. / Popov, V.O. / Sluchanko, N.N. / Boyko, K.M. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and quenching of a bundle-shaped phycobilisome Authors: Burtseva, A.D. / Slonimskiy, Y.B. / Baymukhametov, T.N. / Sinetova, M.A. / Maksimov, E.G. / Popov, V.O. / Boyko, K.M. / Sluchanko, N.N. | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.6 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 6.3 MB | Display | ![]() |
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Full document | ![]() | 7 MB | Display | |
Data in XML | ![]() | 471.8 KB | Display | |
Data in CIF | ![]() | 653.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 64815MC ![]() 9v7gC ![]() 9v7hC ![]() 9v7iC ![]() 9v7kC ![]() 9v7lC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Allophycocyanin ... , 2 types, 80 molecules MOEGIKQSUWYacegikmortwy13579AAAC...
#2: Protein | Mass: 17555.062 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 17241.664 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Phycobilisome ... , 2 types, 8 molecules suAYAZAaAbAcAd
#4: Protein | Mass: 17452.838 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 7765.004 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein / Non-polymers , 2 types, 86 molecules AC

#1: Protein | Mass: 130002.258 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Chemical | ChemComp-CYC / |
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-Details
Has ligand of interest | Y |
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Has protein modification | Y |
-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: Bundle-shaped phycobilisome / Type: COMPLEX / Entity ID: #1, #5 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Buffer solution | pH: 7 |
Buffer component | Conc.: 50 mM / Name: Tris(hydroxymethyl)aminomethane hydrochloride / Formula: Tris-HCl |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS / Details: Preliminary grid screening was performed manually. |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 85000 X / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm / Cs: 0.01 mm / C2 aperture diameter: 100 µm / Alignment procedure: ZEMLIN TABLEAU |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 3.9 sec. / Electron dose: 66 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV Spherical aberration corrector: Microscope was modified with a Cs corrector (CEOS GmbH, Germany). |
Image scans | Width: 5760 / Height: 4092 |
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Processing
EM software | Name: REFMAC / Version: 5.8.0425 / Category: model refinement |
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CTF correction | Type: NONE |
Symmetry | Point symmetry: C2 (2 fold cyclic) |
3D reconstruction | Resolution: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 746972 / Symmetry type: POINT |