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- EMDB-1101: Coat protein fold and maturation transition of bacteriophage P22 ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-1101 | |||||||||
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Title | Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. | |||||||||
![]() | Z-axis along 3fold symmetry axis, Y-axis along 2fold symmetry axis | |||||||||
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Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 9.5 Å | |||||||||
![]() | Jiang W / Li Z / Zhang Z / Baker ML / Prevelige PE / Chiu W | |||||||||
![]() | ![]() Title: Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Authors: Wen Jiang / Zongli Li / Zhixian Zhang / Matthew L Baker / Peter E Prevelige / Wah Chiu / ![]() Abstract: Bacteriophage P22 is a prototypical biological machine used for studying protein complex assembly and capsid maturation. Using cryo-EM, we solved the structures of P22 before and after the capsid ...Bacteriophage P22 is a prototypical biological machine used for studying protein complex assembly and capsid maturation. Using cryo-EM, we solved the structures of P22 before and after the capsid maturation at 8.5 A and 9.5 A resolutions, respectively. These structures allowed visualization of alpha-helices and beta-sheets from which the capsid protein fold is derived. The capsid fold is similar to that of the coat protein of HK97 bacteriophage. The cryo-EM shows that a large conformational change of the P22 capsid during maturation transition involves not only the domain movement of individual subunits, but also refolding of the capsid protein. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 61.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.9 KB 9.9 KB | Display Display | ![]() |
Images | ![]() | 17.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 258.8 KB | Display | ![]() |
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Full document | ![]() | 257.9 KB | Display | |
Data in XML | ![]() | 4.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Z-axis along 3fold symmetry axis, Y-axis along 2fold symmetry axis | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.815 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : P22 Mature Phage
Entire | Name: P22 Mature Phage |
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Components |
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-Supramolecule #1000: P22 Mature Phage
Supramolecule | Name: P22 Mature Phage / type: sample / ID: 1000 / Number unique components: 1 |
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Molecular weight | Experimental: 18 MDa / Theoretical: 18 MDa |
-Supramolecule #1: Enterobacteria phage P22
Supramolecule | Name: Enterobacteria phage P22 / type: virus / ID: 1 / Name.synonym: P22 mature phage / Details: the icosahedral protein shell / NCBI-ID: 10754 / Sci species name: Enterobacteria phage P22 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No / Syn species name: P22 mature phage |
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Host (natural) | Organism: ![]() |
Molecular weight | Experimental: 18 MDa / Theoretical: 18 MDa |
Virus shell | Shell ID: 1 / Name: capsid shell / Diameter: 700 Å / T number (triangulation number): 7 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Grid | Details: 400 mesh copper grid |
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Vitrification | Cryogen name: ETHANE / Chamber temperature: 90 K / Instrument: HOMEMADE PLUNGER / Details: Vitrification instrument: home-made plunger |
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Electron microscopy
Microscope | JEOL 4000EX |
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Temperature | Min: 95 K / Max: 95 K / Average: 95 K |
Alignment procedure | Legacy - Astigmatism: by monitoring Thon rings at very close to focus |
Image recording | Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: ZEISS SCAI / Digitization - Sampling interval: 7 µm / Number real images: 100 / Average electron dose: 30 e/Å2 Details: scanned at 7micrometer then averaged to 14micrometer step size Bits/pixel: 8 |
Tilt angle min | 0 |
Tilt angle max | 0 |
Electron beam | Acceleration voltage: 400 kV / Electron source: LAB6 |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 5.6 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 40000 |
Sample stage | Specimen holder: side entry / Specimen holder model: GATAN LIQUID NITROGEN |
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Image processing
CTF correction | Details: per micrograph |
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Final reconstruction | Applied symmetry - Point group: I (icosahedral) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 9.5 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: SAVR / Number images used: 5600 |
-Atomic model buiding 1
Initial model | PDB ID: ![]() 1fh6 Chain - Chain ID: A |
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Software | Name: foldhunter |
Details | PDBEntryID_givenInChain. Protocol: rigid body |
Refinement | Protocol: RIGID BODY FIT / Target criteria: correlation coefficient |