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- EMDB-39783: Cryo-EM structure of the MS ring (C34) within the polar flagellar... -
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Open data
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Basic information
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Title | Cryo-EM structure of the MS ring (C34) within the polar flagellar motor | ||||||||||||
![]() | Main map | ||||||||||||
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![]() | Polar flagellum / Polar flagellar motor / MS ring / MOTOR PROTEIN | ||||||||||||
Function / homology | ![]() bacterial-type flagellum basal body, MS ring / cytoskeletal motor activity / bacterial-type flagellum-dependent cell motility / plasma membrane Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.93 Å | ||||||||||||
![]() | Zhang L / Tan JX / Zhou Y / Zhu YQ | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of the MS ring (C34) within the polar flagellar motor Authors: Zhang L / Tan JX / Zhou Y / Zhu YQ | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 118 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18.1 KB 18.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 10.5 KB | Display | ![]() |
Images | ![]() | 110.2 KB | ||
Filedesc metadata | ![]() | 5.9 KB | ||
Others | ![]() ![]() | 115.8 MB 115.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 19.1 KB | Display | |
Data in CIF | ![]() | 24.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8z5vMC 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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Related items in Molecule of the Month |
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Map
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Annotation | Main map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.2 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_39783_half_map_1.map | ||||||||||||
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Annotation | Half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map B
File | emd_39783_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 : The polar flagellar motor-hook complex
Entire | Name: The polar flagellar motor-hook complex |
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Components |
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-Supramolecule #1: The polar flagellar motor-hook complex
Supramolecule | Name: The polar flagellar motor-hook complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Flagellar M-ring protein
Macromolecule | Name: Flagellar M-ring protein / type: protein_or_peptide / ID: 1 / Number of copies: 34 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 63.915605 KDa |
Sequence | String: MADKSTDLTV TEGGSDGALV ASSDVDVESQ NPDLEERSAS KFDMAVGDLD LLRQVVLVLS ISICVALIVM LFFWVKEPEM RPLGAYETE ELIPVLDYLD QQKINYKLDG NTISVESSEY NSIKLGMVRS GVNQATEAGD DILLQDMGFG VSQRLEQERL K LSRERQLA ...String: MADKSTDLTV TEGGSDGALV ASSDVDVESQ NPDLEERSAS KFDMAVGDLD LLRQVVLVLS ISICVALIVM LFFWVKEPEM RPLGAYETE ELIPVLDYLD QQKINYKLDG NTISVESSEY NSIKLGMVRS GVNQATEAGD DILLQDMGFG VSQRLEQERL K LSRERQLA QAIEEMKQVR KARVLLALPK HSVFVRHNQE ASASVFLTLS TGTNLKQQEV DSIVDMVASA VPGMKTSRIT VT DQHGRLL SSGSQDPASA ARRKEQELER SQEQALREKI DSVLLPILGY GNYTAQVDIQ MDFSAVEQTR KRFDPNTPAT RSE YALEDY NNGNMVAGIP GALSNQPPAD ASIPQDVAQM KDGSVMGQGS VRKESTRNFE LDTTISHERK QTGTVARQTV SVAI KDRRQ VNPDTGEVTY TPMSESEINA IRQVLIGTVG FDQGRGDLLN VLSVKFAEPE AEQLEEPPIW EHPNFSDWVR WFASA LVII VVVLVLVRPA MKKLLNPTSD DEDEMYGPDG LPIGADGETS LIGSDIESSE LFEFGSSIDL PNLHKDEDVL KAVRAL VAN EPELAAQVVK NWMNDNG UniProtKB: Flagellar M-ring 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 |
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Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 10 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV |
Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
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Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
Output model | ![]() PDB-8z5v: |