Table 1 Cryo-EM data collection, refinement and validation statistics
From: Fascin structural plasticity mediates flexible actin bundle construction
No. 1 Fascin cross-linked F-actin (Multibody: fascin bound filament 1) (EMDB-43364) (PDB 8VO5) | No. 2 Fascin cross-linked F-actin (Multibody: fascin bound filament 2) (EMDB-43365) (PDB 8VO6) | No. 3 Fascin cross-linked F-actin (Composite map) (EMDB-43366) (PDB 8VO7) | No. 4 Fascin cross-linked F-actin (Eigen_left) (EMDB-43367) (PDB 8VO8) | No. 5 Fascin cross-linked F-actin (Eigen_middle) (EMDB-43368) (PDB 8VO9) | No. 6 Fascin cross-linked F-actin (Eigen_right) (EMDB-43369) (PDB 8VOA) | No. 7 Bundle element, 460 Å (EMDB-43370) | No. 8 Bundle element, 740 Å (EMDB-43371) | |
|---|---|---|---|---|---|---|---|---|
Data collection and processing | ||||||||
Magnification | 29,000 | 29,000 | 29,000 | 29,000 | 29,000 | 29,000 | 29,000 | 29,000 |
Voltage (kV) | 300 | 300 | 300 | 300 | 300 | 300 | 300 | 300 |
Electron exposure (e−/Å2) | 61.26 | 61.26 | 61.26 | 61.26 | 61.26 | 61.26 | 61.26 | 61.26 |
Defocus range (μm) | −0.8 to −2.2 | −0.8 to −2.2 | −0.8 to −2.2 | −0.8 to −2.2 | −0.8 to −2.2 | −0.8 to −2.2 | −0.8 to −2.2 | −0.8 to −2.2 |
Pixel size (Å) | 1.03 | 1.03 | 1.03 | 1.03 | 1.03 | 1.03 | 1.03 | 1.03 |
Symmetry imposed | C1 | C1 | C1 | C1 | C1 | C1 | C1 | C1 |
Initial particle images (no.) | 3,056,360 | 3,056,360 | – | 113,800 | 113,800 | 113,800 | 3,056,360 | 3,056,360 |
Final particle images (no.) | 113,800 | 113,800 | – | 17,207 | 79,824 | 16,769 | 8,477 | 8,053 |
Map resolution (Å) | 3.0 | 3.1 | – | 3.9 | 3.4 | 4.0 | 8.7 | 12.0 |
FSC threshold | 0.143 | 0.143 | 0.143 | 0.143 | 0.143 | 0.143 | 0.143 | |
Map resolution range (Å) | 2.9–4.9 | 3.0–4.7 | – | 3.7–6.7 | 3.3–5.3 | 3.7–7.2 | 6.3–13.0 | 7.1–24.7 |
Refinement | ||||||||
Initial model used (PDB code) | – | – | ||||||
Model resolution (Å) | 3.1 | 3.0 | 3.1 | 3.6 | 3.5 | 3.6 | – | – |
FSC threshold | 0.5 | 0.5 | 0.5 | 0.5 | 0.5 | 0.5 | ||
Model resolution range (Å) | N.A. | N.A. | N.A. | N.A. | N.A. | N.A. | – | – |
Map sharpening B factor (Å2) | −55.11 | −48.84 | – | −50.28 | −62.33 | −48.48 | −108.59 | −512.65 |
Model composition | 3 actin protomers, 1 fascin | 3 actin protomers, 1 fascin | 6 actin protomers, 1 fascin | 6 actin protomers, 1 fascin | 6 actin protomers, 1 fascin | 6 actin protomers, 1 fascin | – | – |
Non-hydrogen atoms | 12,625 | 12,625 | 21,460 | 21,460 | 21,460 | 21,460 | – | – |
Protein residues | 1,604 | 1,604 | 2,723 | 2,723 | 2,723 | 2,723 | – | – |
Ligands | 3 Mg.ADP | 3 Mg.ADP | 6 Mg.ADP | 6 Mg.ADP | 6 Mg.ADP | 6 Mg.ADP | – | – |
B factors (Å2) | ||||||||
Protein | 23.94 | 27.87 | 43.13 | 99.43 | 78.72 | 112.12 | – | – |
Ligand | 8.28 | 18.9 | 39.23 | 90.45 | 65.04 | 96.87 | – | – |
R.m.s. deviations | ||||||||
Bond lengths (Å) | 0.003 | 0.005 | 0.004 | 0.004 | 0.002 | 0.004 | – | – |
Bond angles (°) | 0.583 | 0.663 | 0.612 | 0.667 | 0.566 | 0.614 | – | – |
Validation | ||||||||
MolProbity score | 1.55 | 1.73 | 1.55 | 1.94 | 1.63 | 2.07 | – | – |
Clashscore | 7.37 | 8.65 | 8.07 | 16.31 | 8.24 | 18.66 | – | – |
Poor rotamers (%) | 0 | 0 | 0 | 0.04 | 0.07 | 0.09 | – | – |
Ramachandran plot | ||||||||
Favored (%) | 97.23 | 96.16 | 97.44 | 96.58 | 96.92 | 95.62 | – | – |
Allowed (%) | 2.77 | 3.84 | 2.56 | 3.42 | 3.08 | 4.38 | – | – |
Disallowed (%) | 0.00 | 0.00 | 0.00 | 0.00 | 0.00 | 0.00 | – | – |
