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Open data
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Basic information
Entry | ![]() | ||||||||||||
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Title | Structure of flexible tail tube of bacteriophage T1 | ||||||||||||
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![]() | tail tube / phage / VIRUS PROTEIN / VIRAL PROTEIN | ||||||||||||
Function / homology | Phage tail tube protein 3 / Phage tail tube protein, TTP / Putative major tail protein![]() | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.1 Å | ||||||||||||
![]() | Chen Y / Liu HR | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: The in situ structure of T-series T1 reveals a conserved Lambda-like tail tip Authors: Chen Y / Liu HR | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 39.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.7 KB 13.7 KB | Display Display | ![]() |
Images | ![]() | 37.6 KB | ||
Filedesc metadata | ![]() | 5 KB | ||
Others | ![]() ![]() | 39.7 MB 39.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9l0fMC ![]() 9kzjC ![]() 9l01C ![]() 9l0eC ![]() 9l9pC 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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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.36 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_62699_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_62699_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Escherichia phage T1
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Escherichia phage T1
Supramolecule | Name: Escherichia phage T1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Putative major tail protein
Macromolecule | Name: Putative major tail protein / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 24.084053 KDa |
Sequence | String: MHLPNGAQIF VETSRGVEVE ATAITNAENP VATVASKGDL AKGDYVIVTQ STWAKMVSRV LIVTDAQETS ITLAGIDTSD TLVFPAGGT MSFAKITGWT EIPCVQEIGQ DGGEQQYYTY QCLSDDKEQQ IPTFKSAVSL TYTFAHEFDN PIYPILRKLD S SGQVTAVR ...String: MHLPNGAQIF VETSRGVEVE ATAITNAENP VATVASKGDL AKGDYVIVTQ STWAKMVSRV LIVTDAQETS ITLAGIDTSD TLVFPAGGT MSFAKITGWT EIPCVQEIGQ DGGEQQYYTY QCLSDDKEQQ IPTFKSAVSL TYTFAHEFDN PIYPILRKLD S SGQVTAVR MYVPKASEMR MWAGILSFND IPSTQVNEME TVELAVSLKG DFTFISSTLA SPGA UniProtKB: Putative major tail 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: 7.6 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 32.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 4.0 µm / Nominal defocus min: 2.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 34215 |
Initial angle assignment | Type: COMMON LINE |
Final angle assignment | Type: COMMON LINE |