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. Author manuscript; available in PMC: 2020 Jan 8.
Published in final edited form as: Nat Struct Mol Biol. 2019 Jul 8;26(8):671–678. doi: 10.1038/s41594-019-0257-3

Table 1.

Cryo-EM data collection, refinement and validation statistics

SpastinE583Q (PDB 6P07) (EMDB 20226)
Data collection and Processing
Microscope Thermo Fischer Talos Arctica
Camera Gatan K2 Summit DED
Magnification (nominal) 36,000x
Magnification (calibrated) 43478.3x
Voltage (kV) 200
Total electron exposure (e2) 52
Exposure rate (e-/pixel/sec) 5.6
Defocus range (μm) −1.0 to −2.0
Pixel size (Å) 1.15
Micrographs collected (no.) 2,534
Micrographs used (no.) 2,534
Total extracted particles (no.) 2,736,865
Refined particles (no.) 1,259,553
Final particles (no.) 488,385
Symmetry imposed C1
Resolution (global)
 FSC 0.5 (unmasked/masked) 7.0/3.6
 FSC 0.143 (unmasked/masked) 4.3/3.2
Resolution Range (local) 3 – 5
Model composition
Nonhydrogen atoms 14,089
Protein residues 1804
Ligands 12
Refinement
Initial model used (PDB code) 3B9P
Average FSC 3.2
B factors (Å2)
 Protein residues 46.8
 Ligands 50.5
R.m.s. deviations
 Bond lengths (Å) 0.01
 Bond angles (°) 1.14
Validation
MolProbity score 1.46
Clashscore 3.05
Poor rotamers (%) 0.0
C-beta deviations 0
Mean per-residue Cα RMSD (Å) 0.64
Per-residue Cα RMSD range (Å) 0.03–5.66
Ramachandran plot
 Favored (%) 94.65%
 Allowed (%) 5.35%
 Disallowed (%) 0.00%
EMRinger score84 3.00
CaBLAM outliers 3.35%