8a9l

Cryo-EM structure of alpha-synuclein filaments from Parkinson's disease and dementia with Lewy bodies

Method: ELECTRON MICROSCOPY Dmax: 75.8 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Alpha-synuclein

OrganismNot specified

UniProt P37840

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 9 PDB declaration: Trimeric(3) Count mismatch; review required Chain A; UniProt 1–140 Not recorded Unknown fragment × 3 Unknown fragment × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

226 other PDB entries and 234 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYUA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–140; UniProt 1–140

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8a9l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8a9l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8a9l
Deposition date deposition_date2022-06-28
Structure title titleCryo-EM structure of alpha-synuclein filaments from Parkinson's disease and dementia with Lewy bodies
Keywords keywords;alpha-synuclein, amyloid, fibril, Parkinson's disease (PD), Parkinson's disease dementia (PDD), dementia with Lewy bodies (DLB), synucleinopathy, PROTEIN FIBRIL ;; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.11
Radius of gyration Rg (electron density) rg_electron21.58
Forward intensity I(0) i01423070.00
Molecular weight molecular_weight8095.0 kDa
Excluded volume excluded_volume10166 ų
Envelope volume envelope_volume17098 ų
Hydration-shell volume shell_volume7828 ų
Envelope diameter envelope_diameter74.1
Shell Rg shell_rg23.77
Envelope Rg envelope_rg21.33
Shape Rg shape_rg21.61
Total Rg total_rg21.98
Total atoms total_atoms570
Residues n_residues86
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax75.8
Rg (real space) rg_real22.32
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real1.4230e+06
I(0) uncertainty (real space) i0_real_error2.0580e+04
Rg (reciprocal space) rg_reciprocal22.28
I(0) (reciprocal space) i0_reciprocal1423000.0000
Solution quality estimate total_estimate0.6995
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.376
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha156600.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 0.262; Positv: 1.000; Valcen: 0.692; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)