+
Open data
-
Basic information
| Entry | ![]() | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | Murine AA amyloid fibril morphology III (AA III) | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | 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 Function and homology information | |||||||||
| Biological species | ![]() | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Andreotti G / Schmidt M / Faendrich M | |||||||||
| Funding support | Germany, 2 items
| |||||||||
Citation | Journal: J Mol Biol / Year: 2025Title: 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 |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_53573.map.gz | 2.1 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-53573-v30.xml emd-53573.xml | 18.1 KB 18.1 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_53573_fsc_1.xml emd_53573_fsc_2.xml | 10.7 KB 10.7 KB | Display Display | FSC data file |
| Images | emd_53573.png | 34.4 KB | ||
| Masks | emd_53573_msk_1.map | 103 MB | Mask map | |
| Filedesc metadata | emd-53573.cif.gz | 5.5 KB | ||
| Others | emd_53573_additional_1.map.gz emd_53573_half_map_1.map.gz emd_53573_half_map_2.map.gz | 7.6 MB 79.3 MB 79.4 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53573 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53573 | HTTPS FTP |
-Validation report
| Summary document | emd_53573_validation.pdf.gz | 829.7 KB | Display | EMDB validaton report |
|---|---|---|---|---|
| Full document | emd_53573_full_validation.pdf.gz | 829.2 KB | Display | |
| Data in XML | emd_53573_validation.xml.gz | 13.2 KB | Display | |
| Data in CIF | emd_53573_validation.cif.gz | 15.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53573 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-53573 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9r4zMC M: atomic model generated by this map C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|
-
Map
| File | Download / File: emd_53573.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-Mask #1
| File | emd_53573_msk_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Additional map: #1
| File | emd_53573_additional_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #2
| File | emd_53573_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #1
| File | emd_53573_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-
Sample components
-Entire : Amyloid fibril containing SAA peptides
| Entire | Name: Amyloid fibril containing SAA peptides |
|---|---|
| Components |
|
-Supramolecule #1: Amyloid fibril containing SAA peptides
| Supramolecule | Name: Amyloid fibril containing SAA peptides / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
|---|---|
| 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 |
|---|---|
| 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 |
|---|---|
Processing | helical reconstruction |
| Aggregation state | helical array |
-
Sample preparation
| Buffer | pH: 7 / Details: water |
|---|---|
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Instrument: LEICA PLUNGER |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| 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: FIELD EMISSION GUN |
| 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 |
+
Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: OTHER |
|---|---|
| Output model | ![]() PDB-9r4z: |
Movie
Controller
About Yorodumi




Keywords
Authors
Germany, 2 items
Citation

Z (Sec.)
Y (Row.)
X (Col.)




















































FIELD EMISSION GUN

