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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Cryo-EM of rPFFs (recombinant preformed fibrils) | |||||||||
Map data | EMReady sharpened map | |||||||||
Sample |
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Keywords | Amyloid / recombinant preformed fibrils / PROTEIN FIBRIL | |||||||||
| Function / homology | Function and homology informationnegative regulation of mitochondrial electron transport, NADH to ubiquinone / negative regulation of dopamine uptake involved in synaptic transmission / negative regulation of norepinephrine uptake / response to desipramine / positive regulation of SNARE complex assembly / positive regulation of hydrogen peroxide catabolic process / supramolecular fiber / regulation of synaptic vesicle recycling / negative regulation of chaperone-mediated autophagy / regulation of reactive oxygen species biosynthetic process ...negative regulation of mitochondrial electron transport, NADH to ubiquinone / negative regulation of dopamine uptake involved in synaptic transmission / negative regulation of norepinephrine uptake / response to desipramine / positive regulation of SNARE complex assembly / positive regulation of hydrogen peroxide catabolic process / supramolecular fiber / regulation of synaptic vesicle recycling / negative regulation of chaperone-mediated autophagy / regulation of reactive oxygen species biosynthetic process / positive regulation of protein localization to cell periphery / negative regulation of exocytosis / dopamine biosynthetic process / dopamine uptake involved in synaptic transmission / response to iron(II) ion / negative regulation of dopamine metabolic process / negative regulation of platelet-derived growth factor receptor signaling pathway / SNARE complex assembly / negative regulation of thrombin-activated receptor signaling pathway / Lewy body / negative regulation of microtubule polymerization / synaptic vesicle priming / synaptic vesicle transport / regulation of norepinephrine uptake / transporter regulator activity / protein kinase inhibitor activity / positive regulation of inositol phosphate biosynthetic process / regulation of dopamine secretion / positive regulation of receptor recycling / cuprous ion binding / positive regulation of exocytosis / nuclear outer membrane / dynein complex binding / synaptic transmission, dopaminergic / synaptic vesicle exocytosis / response to magnesium ion / positive regulation of endocytosis / negative regulation of serotonin uptake / cysteine-type endopeptidase inhibitor activity / kinesin binding / regulation of presynapse assembly / synaptic vesicle endocytosis / alpha-tubulin binding / beta-tubulin binding / phospholipase binding / behavioral response to cocaine / supramolecular fiber organization / cellular response to fibroblast growth factor stimulus / response to type II interferon / cellular response to epinephrine stimulus / inclusion body / Hsp70 protein binding / response to interleukin-1 / cellular response to copper ion / axon terminus / positive regulation of release of sequestered calcium ion into cytosol / enzyme inhibitor activity / glutathione metabolic process / regulation of microtubule cytoskeleton organization / SNARE binding / protein tetramerization / protein sequestering activity / microglial cell activation / phosphoprotein binding / receptor internalization / tubulin binding / protein destabilization / ferrous iron binding / synapse organization / phospholipid binding / PKR-mediated signaling / tau protein binding / enzyme activator activity / positive regulation of inflammatory response / terminal bouton / actin cytoskeleton / synaptic vesicle membrane / growth cone / actin binding / cellular response to oxidative stress / response to lipopolysaccharide / histone binding / cell cortex / microtubule binding / negative regulation of neuron apoptotic process / amyloid fibril formation / mitochondrial outer membrane / lysosome / oxidoreductase activity / mitochondrial inner membrane / transcription cis-regulatory region binding / positive regulation of apoptotic process / ribosome / mitochondrial matrix / Amyloid fiber formation / copper ion binding / protein domain specific binding / axon / neuronal cell body / calcium ion binding Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 3.05 Å | |||||||||
Authors | Fielding LA / Zia A / Volpicelli-Daley LA / Wang F | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: To Be PublishedTitle: Cryo-EM of rPFFs Authors: Fielding LA / Zia A / Volpicelli-Daley LA / Wang F | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Header (meta data) | emd-77765-v30.xml emd-77765.xml | 15 KB 15 KB | Display Display | EMDB header |
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| FSC (resolution estimation) | emd_77765_fsc.xml | 11.3 KB | Display | FSC data file |
| Images | emd_77765.png | 49.8 KB | ||
| Map data | emd_77765.map.gz | 20.4 MB | EMDB map data format | |
| Masks | emd_77765_msk_1.map | 125 MB | Mask map | |
| Filedesc metadata | emd-77765.cif.gz | 5.2 KB | ||
| Others | emd_77765_half_map_1.map.gz emd_77765_half_map_2.map.gz | 96.6 MB 96.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-77765 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-77765 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 36qdMC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
-Supplemental data
-Mask #1
| File | emd_77765_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: #1
| File | emd_77765_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_77765_half_map_2.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Human alpha-synucelin
| Entire | Name: Human alpha-synucelin |
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| Components |
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-Supramolecule #1: Human alpha-synucelin
| Supramolecule | Name: Human alpha-synucelin / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Alpha-synuclein
| Macromolecule | Name: Alpha-synuclein / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 14.476108 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIA AATGFVKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE A UniProtKB: Alpha-synuclein |
-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 | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 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: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
United States, 1 items
Citation
Z (Sec.)
Y (Row.)
X (Col.)














































Processing
FIELD EMISSION GUN

