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Open data
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Basic information
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Title | Murine AA amyloid fibril morphology III (AA III) | |||||||||
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![]() | Amyloid fibril / AA amyloidosis / systemic amyloidosis / AApoAII amyloidosis / misfolfing disease / protein aggregation / PROTEIN FIBRIL | |||||||||
Function / homology | Serum amyloid A protein / : / Serum amyloid A protein / Serum amyloid A proteins signature. / Serum amyloid A proteins / response to stilbenoid / high-density lipoprotein particle / acute-phase response / Serum amyloid A-2 protein![]() | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Andreotti G / Schmidt M / Faendrich M | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM Observation of AA Amyloid Fibrils in Mouse Model of Systemic AApoAII Amyloidosis. Authors: Giada Andreotti / Keichii Higuchi / Matthias Schmidt / Marcus Fändrich / ![]() ![]() Abstract: The co-deposition of amyloid fibrils from different precursor proteins is a topic of increasing relevance for protein misfolding diseases. Using cryo-electron microscopy (cryo-EM), we here determined ...The co-deposition of amyloid fibrils from different precursor proteins is a topic of increasing relevance for protein misfolding diseases. Using cryo-electron microscopy (cryo-EM), we here determined the structures of two serum amyloid A (SAA) protein-derived amyloid fibril morphologies that were extracted from a mouse strain that is primarily known to be associated with apolipoprotein A-II-derived amyloid fibrils. The two fibril morphologies show the same protomer conformation as in previously reported ex vivo amyloid fibrils from SAA protein but a different relative arrangement of fibril protein stacks. These data establish that serum amyloid A-derived amyloid fibrils share the same fibril protein fold in different mouse strains and disease contexts. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 2.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.4 KB 17.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() ![]() | 10.7 KB 10.7 KB | Display Display | ![]() |
Images | ![]() | 34.4 KB | ||
Masks | ![]() | 103 MB | ![]() | |
Filedesc metadata | ![]() | 5.3 KB | ||
Others | ![]() ![]() ![]() | 7.6 MB 79.3 MB 79.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 829.4 KB | Display | ![]() |
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Full document | ![]() | 828.9 KB | Display | |
Data in XML | ![]() | 13.2 KB | Display | |
Data in CIF | ![]() | 15.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9r4zMC 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
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: #1
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-Half map: #2
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Density Histograms |
-Half map: #1
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Density Histograms |
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Sample components
-Entire : Amyloid fibril containing SAA peptides
Entire | Name: Amyloid fibril containing SAA peptides |
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Components |
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-Supramolecule #1: Amyloid fibril containing SAA peptides
Supramolecule | Name: Amyloid fibril containing SAA peptides / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Serum amyloid A-2 protein
Macromolecule | Name: Serum amyloid A-2 protein / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 11.622629 KDa |
Sequence | String: GFFSFIGEAF QGAGDMWRAY TDMKEAGWKD GDKYFHARGN YDAAQRGPGG VWAAEKISDA RESFQEFFGR GHEDTMADQE ANRHGRSGK DPNYYRPPGL PAKY UniProtKB: Serum amyloid A-2 protein |
-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 / Details: water |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Instrument: LEICA PLUNGER |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Average electron dose: 42.7 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: OTHER |
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Output model | ![]() PDB-9r4z: |