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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 | |||||||||
 Map data | ||||||||||
 Sample | 
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 Keywords | Bacteriophage / caudovirales / siphoviridae / tail complex / delivery device / phage lambda / cryo-EM / VIRAL PROTEIN | |||||||||
| Function / homology |  Function and homology informationsymbiont 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 |  Escherichia phage Lambda (virus) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.86 Å | |||||||||
 Authors | Wang J | |||||||||
| Funding support |   China, 1 items 
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 Citation |  Journal: Structure / Year: 2024Title: 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.  | |||||||||
| History | 
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Structure visualization
| Supplemental images | 
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Downloads & links
-EMDB archive
| Map data |  emd_36677.map.gz | 229.3 MB |  EMDB map data format | |
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| Header (meta data) |  emd-36677-v30.xml emd-36677.xml | 17.7 KB 17.7 KB  | Display Display  |  EMDB header | 
| FSC (resolution estimation) |  emd_36677_fsc.xml | 13.3 KB | Display |  FSC data file | 
| Images |  emd_36677.png | 50.2 KB | ||
| Filedesc metadata |  emd-36677.cif.gz | 5.7 KB | ||
| Others |  emd_36677_half_map_1.map.gz emd_36677_half_map_2.map.gz | 226.6 MB 226.6 MB  | ||
| Archive directory |  http://ftp.pdbj.org/pub/emdb/structures/EMD-36677 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-36677 | HTTPS FTP  | 
-Validation report
| Summary document |  emd_36677_validation.pdf.gz | 731.8 KB | Display |  EMDB validaton report | 
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| Full document |  emd_36677_full_validation.pdf.gz | 731.4 KB | Display | |
| Data in XML |  emd_36677_validation.xml.gz | 21.6 KB | Display | |
| Data in CIF |  emd_36677_validation.cif.gz | 28.2 KB | Display | |
| Arichive directory |  https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36677 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36677 | 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  F&H Search | 
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Links
| EMDB pages |  EMDB (EBI/PDBe) /  EMDataResource | 
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Map
| File |  Download / File: emd_36677.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
 
 Images are generated by Spider.  | ||||||||||||||||||||||||||||||||||||
| 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 | ||||||||||||
| Projections & Slices | 
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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:  Escherichia phage Lambda (virus) | 
-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:  Escherichia phage Lambda (virus) | 
| 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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 Processing | 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:  FIELD EMISSION GUN | 
| 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  | 
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About Yorodumi




Keywords
Escherichia phage Lambda (virus)
Authors
China, 1 items 
Citation










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Processing
FIELD EMISSION GUN

