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Open data
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Basic information
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Title | Cryo-EM structure of bacteriophage phiXacJX1 capsid | |||||||||
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![]() | Xanthomonas phage / capsid / icosahedron / VIRUS | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Guo M / Wang A / Zheng Y / Liu C / Shao Q / Fang Q | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Cryo-EM structures of a Xanthomonas phage: Insights into viral architecture and implications for the model phage HK97. Authors: Mingcheng Guo / Aohan Wang / Yaqi Zheng / Chaoying Liu / Qianqian Shao / Yunfei Deng / Lin Li / Yueting Wang / Xiaofang Wang / Yue Shen / Jun Qian / Xiaofeng Zhou / Qianglin Fang / ![]() Abstract: Xanthomonas bacteria are responsible for disease outbreaks in several hundred plant species, causing significant economic losses. Xanthomonas phages have emerged as a promising biocontrol strategy in ...Xanthomonas bacteria are responsible for disease outbreaks in several hundred plant species, causing significant economic losses. Xanthomonas phages have emerged as a promising biocontrol strategy in managing various important plant diseases caused by Xanthomonas bacteria. However, structural information for Xanthomonas phages has remained limited so far. Here, we present high-resolution cryo-electron microscopy (cryo-EM) structures of the Xanthomonas citri phage ΦXacJX1 from siphoviruses. These structures include atomic models for the head, head-to-tail connector and head-proximal portion of the tail. ΦXacJX1's head and head-to-tail connector components show significant protein sequence and structural homology with those of the model siphophage HK97. However, the in-situ structures of head-to-tail connector of phage HK97 remain unavailable. The presented structures of phage ΦXacJX1 enhance our understanding of Xanthomonas phages and the mature virion of phage HK97. They provide a valuable framework for future structural and functional studies on both Xanthomonas phages and phage HK97. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.1 GB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.2 KB 16.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 23.6 KB | Display | ![]() |
Images | ![]() | 154.1 KB | ||
Masks | ![]() | 1.1 GB | ![]() | |
Filedesc metadata | ![]() | 5.9 KB | ||
Others | ![]() ![]() | 942.3 MB 945.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 31.7 KB | Display | |
Data in CIF | ![]() | 43.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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: 1.372 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Half map: #2
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
-Entire : Xanthomonas phage phiXacJX1
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Xanthomonas phage phiXacJX1
Supramolecule | Name: Xanthomonas phage phiXacJX1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 3374911 / Sci species name: Xanthomonas phage phiXacJX1 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
-Macromolecule #1: major capsid protein gp3
Macromolecule | Name: major capsid protein gp3 / type: protein_or_peptide / ID: 1 Details: This protein corresponds to a novel sequence that is not yet available in UniProt. The current reference for the sequence is GenBank Accession Number: PQ476032.1 Number of copies: 7 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 41.850199 KDa |
Sequence | String: MSDINVINST LANISDSLKA HADRAVKEQE LNASVRAKVD ELLMAQGALQ ADLKAAQQRI AEVEGNGAGG DVQHISIGQQ FVNSDSFKA MAESGGQRGR AELNIKAAIT SLTTNADGSA GATVQTTRLP GIRELPQRRM TIRSLLAQGT MEGNTLEYVR E TGFTNAAA ...String: MSDINVINST LANISDSLKA HADRAVKEQE LNASVRAKVD ELLMAQGALQ ADLKAAQQRI AEVEGNGAGG DVQHISIGQQ FVNSDSFKA MAESGGQRGR AELNIKAAIT SLTTNADGSA GATVQTTRLP GIRELPQRRM TIRSLLAQGT MEGNTLEYVR E TGFTNAAA PVAEGAQKPE SSLKFDLVQT SAKVIAHWMK ASRQILSDSA QLQSFINARL LRGLEVVEEN QLLNGNGTGQ NL LGLLPQA TAFAAPITVA NATAVDRLRL ALLQAQLAEF PATGIVLNPA DWAGIELLKD TQGRYILGNP QGTLAPTLWG LPV VATQAM AAGQFLTGAF DAGAQVFDRW AARVEVATEN QDDFIKNMVT ILAEERLALA VYRPESFIKG SLTAAAAT |
-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 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 26.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 59000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |