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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Brevibacterium linens encapsulin structure | |||||||||
![]() | Brevibacterium linens encapsulin | |||||||||
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![]() | Bacterial protein compartment / STRUCTURAL PROTEIN | |||||||||
Function / homology | Type 1 encapsulin shell protein / Encapsulating protein for peroxidase / : / encapsulin nanocompartment / Type 1 encapsulin shell protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.28 Å | |||||||||
![]() | Allende-Ballestero C / Luque D | |||||||||
![]() | ![]() Title: Three-dimensional cryoEM structure of Brevibacterium linens encapsulin Authors: Allende-Ballestero C / Luque D / Klem R / Cornelissen JJLM / Caston JR | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 80.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 11.8 KB 11.8 KB | Display Display | ![]() |
Images | ![]() | 347.4 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 578 KB | Display | ![]() |
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Full document | ![]() | 577.5 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 7.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7bcvMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Brevibacterium linens encapsulin | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.047 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Encapsulin
Entire | Name: Encapsulin |
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Components |
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-Supramolecule #1: Encapsulin
Supramolecule | Name: Encapsulin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 1.8 MDa |
-Macromolecule #1: Linocin-M18
Macromolecule | Name: Linocin-M18 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: Hydrolases; Acting on peptide bonds (peptidases) |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 28.590695 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: VNNLYRELAP IPGPAWAEIE EEARRTFKRN IAGRRIVDVA GPTGFETSAV TTGHIRDVQS ETSGLQVKQR IVQEYIELRT PFTVTRQAI DDVARGSGDS DWQPVKDAAT TIAMAEDRAI LHGLDAAGIG GIVPGSSNAA VAIPDAVEDF ADAVAQALSV L RTVGVDGP ...String: VNNLYRELAP IPGPAWAEIE EEARRTFKRN IAGRRIVDVA GPTGFETSAV TTGHIRDVQS ETSGLQVKQR IVQEYIELRT PFTVTRQAI DDVARGSGDS DWQPVKDAAT TIAMAEDRAI LHGLDAAGIG GIVPGSSNAA VAIPDAVEDF ADAVAQALSV L RTVGVDGP YSLLLSSAEY TKVSESTDHG YPIREHLSRQ LGAGEIIWAP ALEGALLVST RGGDYELHLG QDLSIGYYSH DS ETVELYL QETFGFLALT DESSVPLSL UniProtKB: Type 1 encapsulin shell protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R2/2 / Material: COPPER/RHODIUM / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE | ||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 38.85 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated defocus max: 3.2 µm / Calibrated defocus min: 1.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.2 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |