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Open data
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Basic information
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Title | Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3 | ||||||||||||
![]() | Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3 | ||||||||||||
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![]() | amyloid-beta / fibril / lipids / PROTEIN FIBRIL | ||||||||||||
Function / homology | ![]() signaling receptor activator activity / Golgi-associated vesicle / clathrin-coated pit / axonogenesis / central nervous system development / heparin binding / growth cone / perikaryon / early endosome / membrane raft ...signaling receptor activator activity / Golgi-associated vesicle / clathrin-coated pit / axonogenesis / central nervous system development / heparin binding / growth cone / perikaryon / early endosome / membrane raft / signaling receptor binding / cell surface / Golgi apparatus / endoplasmic reticulum / extracellular region / nucleus / plasma membrane Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.75 Å | ||||||||||||
![]() | Frieg B / Han M / Giller K / Dienemann C / Riedel D / Becker S / Andreas LB / Griesinger C / Schroeder GF | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structures of lipidic fibrils of amyloid-β (1-40). Authors: Benedikt Frieg / Mookyoung Han / Karin Giller / Christian Dienemann / Dietmar Riedel / Stefan Becker / Loren B Andreas / Christian Griesinger / Gunnar F Schröder / ![]() Abstract: Alzheimer's disease (AD) is a progressive and incurable neurodegenerative disease characterized by the extracellular deposition of amyloid plaques. Investigation into the composition of these plaques ...Alzheimer's disease (AD) is a progressive and incurable neurodegenerative disease characterized by the extracellular deposition of amyloid plaques. Investigation into the composition of these plaques revealed a high amount of amyloid-β (Aβ) fibrils and a high concentration of lipids, suggesting that fibril-lipid interactions may also be relevant for the pathogenesis of AD. Therefore, we grew Aβ40 fibrils in the presence of lipid vesicles and determined their structure by cryo-electron microscopy (cryo-EM) to high resolution. The fold of the major polymorph is similar to the structure of brain-seeded fibrils reported previously. The majority of the lipids are bound to the fibrils, as we show by cryo-EM and NMR spectroscopy. This apparent lipid extraction from vesicles observed here in vitro provides structural insights into potentially disease-relevant fibril-lipid interactions. | ||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 9.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.4 KB 14.4 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 8.9 KB | Display | ![]() |
Images | ![]() | 77.7 KB | ||
Filedesc metadata | ![]() | 5 KB | ||
Others | ![]() ![]() | 45.9 MB 46 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8oweMC ![]() 8ovkC ![]() 8ovmC ![]() 8owdC ![]() 8owjC ![]() 8owkC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3 | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3 (half map 2)
File | emd_17235_half_map_1.map | ||||||||||||
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Annotation | Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3 (half map 2) | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3 (half map 1)
File | emd_17235_half_map_2.map | ||||||||||||
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Annotation | Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3 (half map 1) | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : The L2-L3 amyloid-beta(1-40) fibril in complex with lipids
Entire | Name: The L2-L3 amyloid-beta(1-40) fibril in complex with lipids |
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Components |
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-Supramolecule #1: The L2-L3 amyloid-beta(1-40) fibril in complex with lipids
Supramolecule | Name: The L2-L3 amyloid-beta(1-40) fibril in complex with lipids type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Amyloid-beta A4 protein
Macromolecule | Name: Amyloid-beta A4 protein / type: protein_or_peptide / ID: 1 / Number of copies: 10 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 4.335852 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV UniProtKB: Amyloid-beta A4 protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 6.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |