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. Author manuscript; available in PMC: 2023 Apr 7.
Published in final edited form as: Structure. 2022 Feb 11;30(4):551–563.e4. doi: 10.1016/j.str.2022.01.008

Table 1.

Cryo-EM data collection, processing, and refinement statistics

Deposition ID EMD-24815 EMD-24814 EMD-24816 EMD-24832
PDB: 7S21 PDB: 7S20 PDB: 7S2T PDB: 7S4Q
Data collection
Magnification 130,000 130,000 130,000 130,000
Voltage (kV) 300 300 300 300
Total dose (e/Å) 66 66 46 46
Frame rate 4 frames/sec 4 frames/sec 5 frames/sec 5 frames/sec
Defocus range (μm) −0.6 to −2.6 −0.6 to −2.6 −0.6 to −2.6 −0.6 to −2.6
Pixel size 1.06 1.06 0.537 0.537
Data processing
Symmetry I1 I1 I1 I1
Initial particle number 20706 20706 8139 10357
Final particle number 5183 9309 7961 8512
Resolution (Å) 3.4 3.4 3.5 3.1
FSC threshold 0.143 0.143 0.143 0.143
Refinement
Map sharpening B factor (Å2) −90 −90 −90 −90
Model composition
Non-hydrogen atoms 2041 6364 6677 6659
Protein residues 265 825 862 862
B factors (Å 2 )
Protein 86.41 79.31 97.95 102.02
R.m.s. deviations
Bond length (Å) 0.006 0.005 0.007 0.008
Bond angles (°) 0.765 0.729 0.903 0.928
Validation
Model-to-map fit CC protein 0.84 0.80 0.80 0.81
MolProbity score 2.17 2.30 2.36 2.35
Clashscore 9.87 12.95 14.00 14.00
Sidechain outliers (%) 0.00 0.3 0.9 0.3
Ramachandran
Favored (%) 85.44 83.88 81.88 82.59
Allowed (%) 14.56 16.12 18.00 17.41
Disallowed (%) 0.00 0.00 0.12 0.00