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Open data
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Basic information
Entry | ![]() | ||||||||||||||||||
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Title | Caulobacter crescentus FljM flagellar filament (symmetrized) | ||||||||||||||||||
![]() | FljM (symmetrized) map | ||||||||||||||||||
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![]() | flagellin / flagellar filament / STRUCTURAL PROTEIN | ||||||||||||||||||
Function / homology | Flagellin, C-terminal domain / Bacterial flagellin C-terminal helical region / Flagellin / Flagellin, N-terminal domain / Bacterial flagellin N-terminal helical region / bacterial-type flagellum / structural molecule activity / extracellular region / Flagellin FljM![]() | ||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.11 Å | ||||||||||||||||||
![]() | Sanchez JC / Montemayor EJ / Ploscariu NT / Parrell D / Baumgardt JK / Yang JE / Sibert B / Cai K / Wright ER | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Direct evidence for multi-flagellin filament stabilization via atomic-level architecture of Caulobacter crescentus flagellar filaments Authors: Sanchez JC / Montemayor EJ / Ploscariu NT / Parrell D / Baumgardt JK / Yang JE / Sibert B / Cai K / Wright ER | ||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 53 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.2 KB 17.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.8 KB | Display | ![]() |
Images | ![]() | 114.1 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Filedesc metadata | ![]() | 5.9 KB | ||
Others | ![]() ![]() | 476 MB 476 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 980.6 KB | Display | ![]() |
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Full document | ![]() | 980.2 KB | Display | |
Data in XML | ![]() | 26.5 KB | Display | |
Data in CIF | ![]() | 34.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8uxnMC 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 | FljM (symmetrized) map | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.834 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: FljM (symmetrized) half map 2
File | emd_42770_half_map_1.map | ||||||||||||
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Annotation | FljM (symmetrized) half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: FljM (symmetrized) half map 1
File | emd_42770_half_map_2.map | ||||||||||||
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Annotation | FljM (symmetrized) half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : FljM flagellar filament (symmetrized)
Entire | Name: FljM flagellar filament (symmetrized) |
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Components |
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-Supramolecule #1: FljM flagellar filament (symmetrized)
Supramolecule | Name: FljM flagellar filament (symmetrized) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 0.28 kDa/nm |
-Macromolecule #1: Flagellin FljM
Macromolecule | Name: Flagellin FljM / type: protein_or_peptide / ID: 1 / Number of copies: 44 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 27.95024 KDa |
Sequence | String: MALNSINTNS GALIALQNLN STNAELTQVQ QRINTGKKIG SAKDNGAIWA TAKNQSATAG SMNAVKDSLQ RGQSTIDVAL AAGDTITDL LGKMKEKALA ASDTSLNTAS FNALKSDFDS LRDQITKAAS NAKFNGVSIA DGTTTKLSFL ANSDGSAFTV T AKTLTLGG ...String: MALNSINTNS GALIALQNLN STNAELTQVQ QRINTGKKIG SAKDNGAIWA TAKNQSATAG SMNAVKDSLQ RGQSTIDVAL AAGDTITDL LGKMKEKALA ASDTSLNTAS FNALKSDFDS LRDQITKAAS NAKFNGVSIA DGTTTKLSFL ANSDGSAFTV T AKTLTLGG LGLTATSSFT TAAAAKTMIG TIDTALQTAT NKLASLGTSS TGLDTHLTFV GKLQDSLDAG VGNLVDADLA KE SAKLQSL QTKQQLGVQA LSIANQSSSS ILSLFR UniProtKB: Flagellin FljM |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.4 / Component - Name: phosphate buffered saline |
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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: 95 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 45.0 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 / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |