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- EMDB-50093: Cryo-EM structure of Staphylococcus aureus bacteriophage phi812 t... -
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Open data
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Basic information
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Title | Cryo-EM structure of Staphylococcus aureus bacteriophage phi812 tail in the pre-contraction state - tube and sheath proteins | |||||||||
![]() | Phage phi812 tail in the pre-contraction state - complete; postprocessed map | |||||||||
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![]() | bacteriophage / phage / contractile / phi812 / tail / VIRUS | |||||||||
Function / homology | Major tail sheath protein / Capsid protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.1 Å | |||||||||
![]() | Binovsky J / Siborova M / Skubnik K / Novacek J / Plevka P | |||||||||
Funding support | European Union, ![]()
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![]() | ![]() Title: Cell attachment and tail contraction of S. aureus phage phi812 Authors: Binovsky J / Siborova M / Skubnik K / Novacek J / Plevka P | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 43.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.3 KB 20.3 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.8 KB | Display | ![]() |
Images | ![]() | 219.5 KB | ||
Masks | ![]() | 178 MB | ![]() | |
Filedesc metadata | ![]() | 6.2 KB | ||
Others | ![]() ![]() | 138.5 MB 138.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9f04MC ![]() 9eufC ![]() 9eugC ![]() 9euhC ![]() 9euiC ![]() 9eujC ![]() 9eukC ![]() 9eulC ![]() 9eumC ![]() 9f05C ![]() 9f06C ![]() 9fkoC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Phage phi812 tail in the pre-contraction state - complete; postprocessed map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.075 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: Phage phi812 tail in the pre-contraction state - complete; half2 map
File | emd_50093_half_map_1.map | ||||||||||||
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Annotation | Phage phi812 tail in the pre-contraction state - complete; half2 map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Phage phi812 tail in the pre-contraction state - complete; half1 map
File | emd_50093_half_map_2.map | ||||||||||||
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Annotation | Phage phi812 tail in the pre-contraction state - complete; half1 map | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Staphylococcus phage 812
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Staphylococcus phage 812
Supramolecule | Name: Staphylococcus phage 812 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 307898 / Sci species name: Staphylococcus phage 812 / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
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-Supramolecule #2: Tail
Supramolecule | Name: Tail / type: complex / ID: 2 / Parent: 1 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Supramolecule #3: Tail tube
Supramolecule | Name: Tail tube / type: complex / ID: 3 / Parent: 2 / Macromolecule list: #2 |
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Source (natural) | Organism: ![]() |
-Supramolecule #4: Tail sheath
Supramolecule | Name: Tail sheath / type: complex / ID: 4 / Parent: 2 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Major tail sheath protein
Macromolecule | Name: Major tail sheath protein / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 64.559008 KDa |
Sequence | String: MAVEPFPRRP ITRPHASIEV DTSGIGGSAG SSEKVFCLIG QAEGGEPNTV YELRNYSQAK RLFRSGELLD AIELAWGSNP NYTAGRILA MRIEDAKPAS AEIGGLKITS KIYGNVANNI QVGLEKNTLS DSLRLRVIFQ DDRFNEVYDN IGNIFTIKYK G EEANATFS ...String: MAVEPFPRRP ITRPHASIEV DTSGIGGSAG SSEKVFCLIG QAEGGEPNTV YELRNYSQAK RLFRSGELLD AIELAWGSNP NYTAGRILA MRIEDAKPAS AEIGGLKITS KIYGNVANNI QVGLEKNTLS DSLRLRVIFQ DDRFNEVYDN IGNIFTIKYK G EEANATFS VEHDEETQKA SRLVLKVGDQ EVKSYDLTGG AYDYTNAIIT DINQLPDFEA KLSPFGDKNL ESSKLDKIEN AN IKDKAVY VKAVFGDLEK QTAYNGIVSF EQLNAEGEVP SNVEVEAGEE SATVTATSPI KTIEPFELTK LKGGTNGEPP ATW ADKLDK FAHEGGYYIV PLSSKQSVHA EVASFVKERS DAGEPMRAIV GGGFNESKEQ LFGRQASLSN PRVSLVANSG TFVM DDGRK NHVPAYMVAV ALGGLASGLE IGESITFKPL RVSSLDQIYE SIDLDELNEN GIISIEFVRN RTNTFFRIVD DVTTF NDKS DPVKAEMAVG EANDFLVSEL KVQLEDQFIG TRTINTSASI IKDFIQSYLG RKKRDNEIQD FPAEDVQVIV EGNEAR ISM TVYPIRSFKK ISVSLVYKQQ TLQA UniProtKB: Major tail sheath protein |
-Macromolecule #2: Capsid protein
Macromolecule | Name: Capsid protein / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 15.94297 KDa |
Sequence | String: MASEAKQTVH TGNTVLLMIK GKPVGRAQSA SGQREYGTTG VYEIGSIMPQ EHVYLRYEGT ITVERLRMKK ENFADLGYAS LGEEILKKD IIDILVVDNL TKQVIISYHG CSANNYNETW QTNEIVTEEI EFSYLTASDK ART UniProtKB: Capsid protein |
-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: 8 / Details: 50mM Tris, 10mM NaCl, 10mM CaCl2 |
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Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Average exposure time: 1.0 sec. / Average electron dose: 48.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 75000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |