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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Salmonella cap-filament complex | |||||||||
![]() | The EM map of cap-filament complex of Salmonella enterica at its native context | |||||||||
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![]() | FliC / FliD / cap / filament / flagella / flagellin / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() bacterial-type flagellum filament cap / bacterial-type flagellum hook / bacterial-type flagellum / bacterial-type flagellum-dependent cell motility / cell adhesion / structural molecule activity / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
![]() | Qin K / Einenkel R / Erhardt M / Bergeron JRC | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure of the complete extracellular bacterial flagellum reveals mechanism for flagellin incorporation Authors: Qin K / Einenkel R / Al-Otaibi NS / Schmidt J / Mann D / Drobnic T / Cohen EJ / Gonzalez-Rodriguez N / Harrowell J / Shmakova E / Beeby M / Erhardt M / Bergeron JRC | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 450.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.1 KB 16.1 KB | Display Display | ![]() |
Images | ![]() | 95.5 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() | 442.8 MB 442.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9gnzMC ![]() 9go6C ![]() 9gsxC 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 | The EM map of cap-filament complex of Salmonella enterica at its native context | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.078 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_51486_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_51486_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 : Flagella
Entire | Name: Flagella |
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Components |
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-Supramolecule #1: Flagella
Supramolecule | Name: Flagella / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Flagellin
Macromolecule | Name: Flagellin / type: protein_or_peptide / ID: 1 / Number of copies: 17 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 51.654344 KDa |
Sequence | String: MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG LTQASRNAND GISIAQTTEG ALNEINNNL QRVRELAVQS ANSTNSQSDL DSIQAEITQR LNEIDRVSGQ TQFNGVKVLA QDNTLTIQVG ANDGETIDID L KQINSQTL ...String: MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG LTQASRNAND GISIAQTTEG ALNEINNNL QRVRELAVQS ANSTNSQSDL DSIQAEITQR LNEIDRVSGQ TQFNGVKVLA QDNTLTIQVG ANDGETIDID L KQINSQTL GLDTLNVQQK YKVSDTAATV TGYADTTIAL DNSTFKASAT GLGGTDQKID GDLKFDDTTG KYYAKVTVTG GT GKDGYYE VSVDKTNGEV TLAGGATSPL TGGLPATATE DVKNVQVANA DLTEAKAALT AAGVTGTASV VKMSYTDNNG KTI DGGLAV KVGDDYYSAT QNKDGSISIN TTKYTADDGT SKTALNKLGG ADGKTEVVSI GGKTYAASKA EGHNFKAQPD LAEA AATTT ENPLQKIDAA LAQVDTLRSD LGAVQNRFNS AITNLGNTVN NLTSARSRIE DSDYATEVSN MSRAQILQQA GTSVL AQAN QVPQNVLSLL R UniProtKB: Flagellin |
-Macromolecule #2: Flagellar hook-associated protein 2
Macromolecule | Name: Flagellar hook-associated protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 5 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 49.887594 KDa |
Sequence | String: MASISSLGVG SNLPLDQLLT DLTKNEKGRL TPITKQQSAN SAKLTAYGTL KSALEKFQTA NTALNKADLF KSTVASSTTE DLKVSTTAG AAAGTYKINV TQLAAAQSLA TKTTFATTKE QLGDTSVTSR TIKIEQPGRK EPLEIKLDKG DTSMEAIRDA I NDADSGIA ...String: MASISSLGVG SNLPLDQLLT DLTKNEKGRL TPITKQQSAN SAKLTAYGTL KSALEKFQTA NTALNKADLF KSTVASSTTE DLKVSTTAG AAAGTYKINV TQLAAAQSLA TKTTFATTKE QLGDTSVTSR TIKIEQPGRK EPLEIKLDKG DTSMEAIRDA I NDADSGIA ASIVKVKENE FQLVLTANSG TDNTMKITVE GDTKLNDLLA YDSTTNTGNM QELVKAENAK LNVNGIDIER QS NTVTDAP QGITLTLTKK VTDATVTVTK DDTKAKEAIK SWVDAYNSLV DTFSSLTKYT AVEPGEEASD KNGALLGDSV VRT IQTGIR AQFANSGSNS AFKTMAEIGI TQDGTSGKLK IDDDKLTKVL KDNTAAAREL LVGDGKETGI TTKIATEVKS YLAD DGIID NAQDNVNATL KSLTKQYLSV SNSIDETVAR YKAQFTQLDT MMSKLNNTSS YLTQQFTAMN KS UniProtKB: Flagellar hook-associated protein 2 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 43.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.7 µm / Nominal defocus min: 0.9 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 15225 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |