Table 1 Statistics of cryo-EM data collection and refinement.
From: The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type α-synuclein
Name | G51D fibril | WT51cs fibril | WTwts fibril |
|---|---|---|---|
PDB | 7E0F | n/a | n/a |
EMDB | EMD-30931 | n/a | n/a |
Data collection | |||
Magnification | 22,500 | 22,500 | 22,500 |
Pixel size (Å) | 1.06 | 1.06 | 1.06 |
Defocus range (μm) | −1 to −2 | −1 to −2 | −1 to −2 |
Voltage (kV) | 300 | 300 | 300 |
Detector | K3 | K3 | K3 |
Microscope | Titan Krios | Titan Krios | Titan Krios |
Exposure time (s per frame) | 0.097 | 0.097 | 0.097 |
Number of frames | 32 | 32 | 32 |
Total dose (e− per Å2) | 55 | 55 | 55 |
Reconstruction | |||
Micrographs | 1869 | 725 | 1056 |
Manually picked fibrils | 28,988 | 12,428 | 7903 |
Box size (pixel) | 288 | 686 | 686 |
Inter-box distance (Å) | 30.5 | 72.7 | 72.7 |
Initial particle images (no.) | 349,716 | 90,963 | 74,598 |
Final particle images (no.) | 213,348 | 40,587 | 16,120 |
Map resolution (Å) | 2.96 | n/a | n/a |
FSC threshold | 0.143 | n/a | n/a |
Map resolution (Å) | 3.15 | n/a | n/a |
FSC threshold | 0.5 | n/a | n/a |
Map sharpening B-factor (Å2) | −144.573 | n/a | n/a |
Helical rise (Å) | 2.43 | n/a | n/a |
Helical twist (°) | −179.37 | n/a | n/a |
Refinement | |||
Initial model used | 6L4S | n/a | n/a |
non-hydrogen atoms | 2, 022 | n/a | n/a |
Protein residues | 294 | n/a | n/a |
Ligands | 0 | n/a | n/a |
r.m.s.d. bond lengths | 0.016 | n/a | n/a |
r.m.s.d. bond angles | 0.986 | n/a | n/a |
All-atom clash score | 9.76 | n/a | n/a |
Rotamer outliers | 0.00% | n/a | n/a |
Ramachandran outliers | 0.00% | n/a | n/a |
Ramachandran allowed | 12.77% | n/a | n/a |
Ramachandran favored | 87.23% | n/a | n/a |