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Open data
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Basic information
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| Title | Type Ib beta-amyloid 42 Filaments from Human Brain | |||||||||
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Sample |
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| Biological species | Homo sapiens (human) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | Yang Y / Arseni D / Zhang W / Huang M / Lovestam SKA / Schweighauser M / Kotecha A / Murzin AG / Peak-Chew SY / Macdonald J ...Yang Y / Arseni D / Zhang W / Huang M / Lovestam SKA / Schweighauser M / Kotecha A / Murzin AG / Peak-Chew SY / Macdonald J / Lavenir I / Garringer HJ / Gelpi E / Newell KL / Kovacs GG / Vidal R / Ghetti B / Falcon B / Scheres HW / Goedert M | |||||||||
| Funding support | United Kingdom, United States, 2 items
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Citation | Journal: Science / Year: 2022Title: Cryo-EM structures of amyloid-β 42 filaments from human brains. Authors: Yang Yang / Diana Arseni / Wenjuan Zhang / Melissa Huang / Sofia Lövestam / Manuel Schweighauser / Abhay Kotecha / Alexey G Murzin / Sew Y Peak-Chew / Jennifer Macdonald / Isabelle Lavenir ...Authors: Yang Yang / Diana Arseni / Wenjuan Zhang / Melissa Huang / Sofia Lövestam / Manuel Schweighauser / Abhay Kotecha / Alexey G Murzin / Sew Y Peak-Chew / Jennifer Macdonald / Isabelle Lavenir / Holly J Garringer / Ellen Gelpi / Kathy L Newell / Gabor G Kovacs / Ruben Vidal / Bernardino Ghetti / Benjamin Ryskeldi-Falcon / Sjors H W Scheres / Michel Goedert / ![]() Abstract: Filament assembly of amyloid-β peptides ending at residue 42 (Aβ42) is a central event in Alzheimer’s disease. Here, we report the cryo–electron microscopy (cryo-EM) structures of Aβ42 ...Filament assembly of amyloid-β peptides ending at residue 42 (Aβ42) is a central event in Alzheimer’s disease. Here, we report the cryo–electron microscopy (cryo-EM) structures of Aβ42 filaments from human brains. Two structurally related S-shaped protofilament folds give rise to two types of filaments. Type I filaments were found mostly in the brains of individuals with sporadic Alzheimer’s disease, and type II filaments were found in individuals with familial Alzheimer’s disease and other conditions. The structures of Aβ42 filaments from the brain differ from those of filaments assembled in vitro. By contrast, in knock-in mice, Aβ42 deposits were made of type II filaments. Knowledge of Aβ42 filament structures from human brains may lead to the development of inhibitors of assembly and improved imaging agents. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_16434.map.gz | 8.9 MB | EMDB map data format | |
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| Header (meta data) | emd-16434-v30.xml emd-16434.xml | 14.4 KB 14.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_16434_fsc.xml | 7.2 KB | Display | FSC data file |
| Images | emd_16434.png | 61.1 KB | ||
| Others | emd_16434_half_map_1.map.gz emd_16434_half_map_2.map.gz | 10.3 MB 10.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-16434 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-16434 | HTTPS FTP |
-Validation report
| Summary document | emd_16434_validation.pdf.gz | 603.6 KB | Display | EMDB validaton report |
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| Full document | emd_16434_full_validation.pdf.gz | 603.2 KB | Display | |
| Data in XML | emd_16434_validation.xml.gz | 12.9 KB | Display | |
| Data in CIF | emd_16434_validation.cif.gz | 17.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16434 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-16434 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_16434.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.93 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_16434_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_16434_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : beta-amyloid 42 filaments extracted from the human brain with Alz...
| Entire | Name: beta-amyloid 42 filaments extracted from the human brain with Alzheimer's disease |
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| Components |
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-Supramolecule #1: beta-amyloid 42 filaments extracted from the human brain with Alz...
| Supramolecule | Name: beta-amyloid 42 filaments extracted from the human brain with Alzheimer's disease type: tissue / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: beta-amyloid 42
| Macromolecule | Name: beta-amyloid 42 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Sequence | String: DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV IA |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | helical reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7.5 |
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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: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Homo sapiens (human)
Authors
United Kingdom,
United States, 2 items
Citation





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




































Processing
FIELD EMISSION GUN

