10xu

Structure of amplified aSyn filament by using seed amplification assay (SAA) from MSA patient CSF.

Method: ELECTRON MICROSCOPY Dmax: 96.7 Å Quality: GOOD

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

Alpha-synuclein

Homo sapiens

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 homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 35–101 Chain B; UniProt 35–101 Chain C; UniProt 35–101 Chain D; UniProt 35–101 Chain E; UniProt 35–101 Chain U; UniProt 35–101 Chain W; UniProt 35–101 Chain X; UniProt 35–101 Chain Y; UniProt 35–101 Chain Z; UniProt 35–101 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 1–67; UniProt 35–101 Author chain B; PDBConstruct 1–67; UniProt 35–101 Author chain C; PDBConstruct 1–67; UniProt 35–101 Author chain D; PDBConstruct 1–67; UniProt 35–101 Author chain E; PDBConstruct 1–67; UniProt 35–101 Author chain U; PDBConstruct 1–67; UniProt 35–101 Author chain W; PDBConstruct 1–67; UniProt 35–101 Author chain X; PDBConstruct 1–67; UniProt 35–101 Author chain Y; PDBConstruct 1–67; UniProt 35–101 Author chain Z; PDBConstruct 1–67; UniProt 35–101

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 10xu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10xu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10xu
Deposition date deposition_date2026-02-11
Structure title titleStructure of amplified aSyn filament by using seed amplification assay (SAA) from MSA patient CSF.
Keywords keywordsaSyn filament, Seed amplification assay, amyloid filament, Prion strain, Prion like propagation, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.66
Radius of gyration Rg (electron density) rg_electron29.50
Forward intensity I(0) i062639200.00
Molecular weight molecular_weight62852.0 kDa
Excluded volume excluded_volume79371 ų
Envelope volume envelope_volume101150 ų
Hydration-shell volume shell_volume30120 ų
Envelope diameter envelope_diameter99.7
Shell Rg shell_rg35.12
Envelope Rg envelope_rg29.32
Shape Rg shape_rg29.52
Total Rg total_rg29.98
Total atoms total_atoms4420
Residues n_residues640
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 dmax96.7
Rg (real space) rg_real29.69
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real6.2640e+07
I(0) uncertainty (real space) i0_real_error9.7950e+05
Rg (reciprocal space) rg_reciprocal29.68
I(0) (reciprocal space) i0_reciprocal62640000.0000
Solution quality estimate total_estimate0.8823
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11660000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.778

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (2)

9. Files and Curves (10)