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- EMDB-19962: Archaellum filament from the Halobacterium salinarum deltaAgl27 strain -
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Open data
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Basic information
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Title | Archaellum filament from the Halobacterium salinarum deltaAgl27 strain | |||||||||
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![]() | archaellum / haloarcheon / archaellin / STRUCTURAL PROTEIN | |||||||||
Biological species | ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.33 Å | |||||||||
![]() | Grossman-Haham I / Shahar A | |||||||||
Funding support | 1 items
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![]() | ![]() Title: Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility Authors: Mashni L / Vershinin Z / Zalk R / Shahar A / Eichler J / Grossman-Haham I | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 141.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.8 KB 15.8 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 13.8 KB | Display | ![]() |
Images | ![]() | 162.3 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() ![]() | 233.9 MB 255.2 MB 255.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 22.9 KB | Display | |
Data in CIF | ![]() | 29.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9etuMC ![]() 9eq7C ![]() 9esmC M: atomic model generated by this map C: citing same article ( |
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Links
EMDB pages | ![]() ![]() |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.89 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: #1
File | emd_19962_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_19962_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_19962_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Archaellum filament
Entire | Name: Archaellum filament |
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Components |
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-Supramolecule #1: Archaellum filament
Supramolecule | Name: Archaellum filament / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 20.466 KDa |
-Macromolecule #1: Archaellin
Macromolecule | Name: Archaellin / type: protein_or_peptide / ID: 1 Details: Since Hbt. salinarum encodes five archaellins (i.e., FlaA1, FlaA2, FlaB1, FlaB2, and FlaB3) and their arrangement within the archaellum filaments is unknown, we further refined the cryo-EM ...Details: Since Hbt. salinarum encodes five archaellins (i.e., FlaA1, FlaA2, FlaB1, FlaB2, and FlaB3) and their arrangement within the archaellum filaments is unknown, we further refined the cryo-EM map without applying symmetry, in an attempt to resolve the positions of these archaellins within the filament, as done previously with reconstruction of the Methanocaldococcus villosus archaellum. Symmetry-free refinement improved the overall resolution map to 3.1 A and revealed differences in density among archaellin subunits. Nonetheless, we were unable to identify features that would allow us to unambiguously assign specific archaellins into the density, perhaps because the regions that distinguish each archaellin are few, short, and mostly predicted to lack defined secondary structure, or because the five archaellins are not organized in a repeating pattern. Consequently, we built a model into the central region of the cryo-EM map comprising 26 archaellin subunits that share a consensus sequence, in which identical residues among the five archaellins are explicitly modelled, with those variable residues usually being modelled as alanine residues (UNK). Number of copies: 25 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 20.107971 KDa |
Sequence | String: MFEFITDEDE RGQVGIGTLI VFIAMVLVAA IAAGVLINTA GYLQSKGSAT GEEASAQVSN RINIVSAYGN V(UNK) (UNK)(UNK)(UNK)VDYV NLTVRQAAGA DNINL(UNK)KSTI QWIGPD(UNK)ATT LTY(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK) ...String: MFEFITDEDE RGQVGIGTLI VFIAMVLVAA IAAGVLINTA GYLQSKGSAT GEEASAQVSN RINIVSAYGN V(UNK) (UNK)(UNK)(UNK)VDYV NLTVRQAAGA DNINL(UNK)KSTI QWIGPD(UNK)ATT LTY(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)ENFTT(UNK)S IKG(UNK)(UNK)(UNK)(UNK)VLV DQSDRIKVIM YA(UNK) (UNK)V(UNK)(UNK)(UNK)L (UNK)(UNK)G(UNK)EVQLTV TTQYGSKTTY WAQVPESLKD KNAV(UNK)L |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | helical array |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: OTHER / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm |