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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Structure of the Evo-Phi36 bacteriophage | |||||||||
Map data | Structure of the Evo-Phi36 bacteriophage | |||||||||
Sample |
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Keywords | Phage / AI / Icosahedral / Evo / VIRUS | |||||||||
| Biological species | Sinsheimervirus / synthetic construct (others) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Li DB / King SH / Driscoll CL / Wilkinson ME / Hie BL | |||||||||
| Funding support | 1 items
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Citation | Journal: Science / Year: 2026Title: Generative design of bacteriophages with genome language models. Authors: Samuel H King / Claudia L Driscoll / David B Li / Daniel Guo / Aditi T Merchant / Garyk Brixi / Max E Wilkinson / Brian L Hie / ![]() Abstract: Many important biological functions arise not from single genes but from complex interactions encoded by entire genomes. We report the first generative design of complete bacteriophage genomes using ...Many important biological functions arise not from single genes but from complex interactions encoded by entire genomes. We report the first generative design of complete bacteriophage genomes using genome language models. We generated viable bacteriophages with target host tropism, using the phage ΦX174 as our design template. Experimental testing yielded 16 phages with diverse fitness profiles in laboratory conditions. Cryo-electron microscopy confirmed that a generated phage utilizes an evolutionarily distant DNA packaging protein in its capsid. A cocktail of generated phages rapidly overcomes ΦX174-resistant strains, demonstrating a path toward artificial intelligence-generated phage therapies against rapidly evolving bacterial pathogens. This work provides a blueprint for the design of diverse synthetic bacteriophages and useful biological systems at the genome scale. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_77391.map.gz | 254.2 MB | EMDB map data format | |
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| Header (meta data) | emd-77391-v30.xml emd-77391.xml | 25.2 KB 25.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_77391_fsc.xml | 18.1 KB | Display | FSC data file |
| Images | emd_77391.png | 101.3 KB | ||
| Filedesc metadata | emd-77391.cif.gz | 6.8 KB | ||
| Others | emd_77391_half_map_1.map.gz emd_77391_half_map_2.map.gz | 475.9 MB 475.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-77391 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-77391 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_77391.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Structure of the Evo-Phi36 bacteriophage | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.923 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Half Map A
| File | emd_77391_half_map_1.map | ||||||||||||
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| Annotation | Half Map A | ||||||||||||
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| Density Histograms |
-Half map: Half Map B
| File | emd_77391_half_map_2.map | ||||||||||||
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| Annotation | Half Map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : synthetic construct
| Entire | Name: synthetic construct (others) |
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| Components |
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-Supramolecule #1: synthetic construct
| Supramolecule | Name: synthetic construct / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Purified from E. coli culture / NCBI-ID: 32630 / Sci species name: synthetic construct / Sci species strain: Evo-Phi36 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: DNA-binding protein J
| Macromolecule | Name: DNA-binding protein J / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Sinsheimervirus |
| Molecular weight | Theoretical: 2.822318 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MKKSIRRSGG KSKGARLWYV GGTQY |
-Macromolecule #2: Capsid protein F
| Macromolecule | Name: Capsid protein F / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Sinsheimervirus |
| Molecular weight | Theoretical: 48.543477 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSNVQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA IDSTVDIFTF YVPHRHVYGE QWIQFMKDG VNASPLPTVN TTGYIDHAAF LGTINPDTNK IPKHLFQGYL NIYNNYFKAP WMPDRTEANP NELNQDDARY G FRCCHLKN ...String: MSNVQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL RLSPLRRGLA IDSTVDIFTF YVPHRHVYGE QWIQFMKDG VNASPLPTVN TTGYIDHAAF LGTINPDTNK IPKHLFQGYL NIYNNYFKAP WMPDRTEANP NELNQDDARY G FRCCHLKN IWTAPLPPET ELSRQMTTST TSIDIMGLQA AYANLHTDQE RDYFMQRYRD VISSFGGKTS YDADNRPLLV MR SNFWASG YDVDGTDQTS LGQFSGRVQQ TYKHSVPRFF VPEHGTMFTL ALVRFPPTAT KEIQYLNAKG ALTYTDIAGD PAL YGNLPP REISMKDVFR SGDASKKFKI AEGQWYRYAP SYVSPVYHLL EGFPFIQEPP SGDLQERVLI RHHDYDQCFQ SVQL LQWNS QVKFNVTVYR NLPTTRDSIM TS |
-Macromolecule #3: Major spike protein G
| Macromolecule | Name: Major spike protein G / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Sinsheimervirus |
| Molecular weight | Theoretical: 19.046637 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MFQTFISRHN SNFFSDKLVA SSVTPASLAP VLQTPKATSS TLYFDSLTVN AANGGFLHCI QMDTSVNAAN QVVSVGADIA FDADPKFFA CLVRFESSSV PTTLPTAYDV YPLDGRHDGG YYTVKDCVTI DVLPRTPGNN VYVGFMVWSN FTATKCRGLV S LNQVIKEI ICLQPLK |
-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: 7.4 Component:
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 150000 |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: AlphaFold / Chain - Initial model type: in silico model |
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| Output model | ![]() PDB-36cr: |
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Keywords
Sinsheimervirus
Authors
Citation



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FIELD EMISSION GUN
