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. 2023 Aug 8;42(18):e114654. doi: 10.15252/embj.2023114654

Table 3.

Summary of cryo‐EM data collection, refinement, and validation statistics.

EM data collection and processing
Microscope Titan Krios
Camera K3
Voltage (kV) 300
Magnification ×105,000
Frames (no.) 35
Total electron dose (e2) 51
Calibrated pixel size (Å) 0.832
Defocus range (μm) 1–2.2
Movies 3,845
Initial picks (no.) 3,271,302
Refined particles (no.) 31,420
Symmetry imposed C1
Global resolution (Å)
FSC 0.5 (unmasked/masked) 7.0/3.2
FSC 0.143 (unmasked/masked) 3.8/2.9
Local resolution range (Å) 2.7–5.2
Map sharpening B factor (Å2) −80
EMD accession number EMD‐40522
Model refinement and validation
Initial models 3LZ0 (nucleosome); Vasudevan et al, 2010
8SIU (ORCAWD40·Orc2N)
Model composition
Non‐hydrogen atoms 14,844
Protein residues 1,118
DNA residues 294
Root mean square deviation
Bond lengths (Å) 0.006
Bond angles (°) 0.854
B factors (Å2)
Protein 62.78
DNA 55.46
Ramachandran plot
% favored 97.24
% allowed 2.76
% outliers 0.0
Rotamer outliers (%) 1.38
MolProbity
Clashscore 5.69
MolProbity score 1.56
Model‐map comparison
EM Ringer score 3.65
CCmask 0.83
FSCmodel/map 0.5 3.1
PDB accession number 8SIY