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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | AHS-CSF domains of phage lambda tail | |||||||||
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![]() | Bacteriophage / caudovirales / siphoviridae / tail complex / delivery device / phage lambda / cryo-EM / VIRAL PROTEIN | |||||||||
Function / homology | ![]() symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / virus tail / host cell cytoplasm / entry receptor-mediated virion attachment to host cell / receptor-mediated virion attachment to host cell / virion attachment to host cell Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.86 Å | |||||||||
![]() | Wang J | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Architecture of the bacteriophage lambda tail. Authors: Chang Wang / Jinsong Duan / Zhiwei Gu / Xiaofei Ge / Jianwei Zeng / Jiawei Wang / ![]() Abstract: Bacteriophage lambda has a double-stranded DNA genome and a long, flexible, non-contractile tail encoded by a contiguous block of 11 genes downstream of the head genes. The tail allows host ...Bacteriophage lambda has a double-stranded DNA genome and a long, flexible, non-contractile tail encoded by a contiguous block of 11 genes downstream of the head genes. The tail allows host recognition and delivery of viral DNA from the head shell to the cytoplasm of the infected cell. Here, we present a high-resolution structure of the tail complex of bacteriophage lambda determined by cryoelectron microscopy. Most component proteins of the lambda tail were determined at the atomic scale. The structure sheds light on the molecular organization of the extensively studied tail of bacteriophage lambda. | |||||||||
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 229.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.8 KB 13.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.3 KB | Display | ![]() |
Images | ![]() | 50.2 KB | ||
Filedesc metadata | ![]() | 4.9 KB | ||
Others | ![]() ![]() | 226.6 MB 226.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 731.8 KB | Display | ![]() |
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Full document | ![]() | 731.4 KB | Display | |
Data in XML | ![]() | 21.6 KB | Display | |
Data in CIF | ![]() | 28.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8jvmMC ![]() 8iydC ![]() 8iykC ![]() 8iylC ![]() 8kgeC C: citing same article ( M: atomic model generated by this map |
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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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Voxel size | X=Y=Z: 1.0742 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: half 1
File | emd_36677_half_map_1.map | ||||||||||||
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Annotation | half 1 | ||||||||||||
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Density Histograms |
-Half map: half 2
File | emd_36677_half_map_2.map | ||||||||||||
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Annotation | half 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : bacteriophage lambda tail
Entire | Name: bacteriophage lambda tail |
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Components |
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-Supramolecule #1: bacteriophage lambda tail
Supramolecule | Name: bacteriophage lambda tail / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Tip attachment protein J
Macromolecule | Name: Tip attachment protein J / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 17.734773 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: ELLEKVELTE DNASRLEEFS KEWKDASDKW NAMAAVKAEQ TKDGKHYVAG IGLSMEDTEE GKLSQFLVAA NRIAAIDPAN GNETPMFVA QGNQIFMNDV FLKRLTAPTI TSGGNPPAFS LTPDGKLTAK NADISGSVNA NSGTLSNVTI AENCTINGTL R AEKIVG UniProtKB: Tip attachment protein J |
-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 |
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Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |