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. 2017 Jun 23;36(14):2073–2087. doi: 10.15252/embj.201696105

Table 1.

Data collection, refinement, and validation statistics

Data collection
Microscope Titan Krios S‐FEG
Camera CMOS (Falcon II)
Voltage (kV) 300
Magnification 59,000×
Pixel size (Å.px−1) 1.1
Defocus range (μm) (−4.5) – (−0.6)
Total dose (ē/Å2) 60
Dose per frame ~3.5
Refinement (tight; loose) dimer/(unrotated; rotated) monomer
Number of particles (total) 132,000/348,000
Number of particles (used for 3D reconstruction) 17,500; 17,300/83,000; 80,000
Resolution (Å; at FSC = 0.143) 11.0; 9.0/3.7; 3.7
CC (model to map fita) n.d.; n.d./0.73; 0.74
Model composition (unrotated; rotated) monomer
Non‐hydrogen atoms 141,613; 141,636
Residues 10,090; 10,093
RMS deviations
Bonds (Å) 0.01; 0.01
Angles (°) 1.08; 1.2
Chirality (°) 0.05; 0.08
Planarity (°) 0.005; 0.007
Validation b
Clashscorec 6.48 (89th p.); 7.82 (82nd p.)
Proteins
MolProbity score 2.06 (72nd p.); 2.16 (67th p.)
Favored rotamers 4,502 (96.22%); 4,400 (94.00%)
Ramachandran favored 4,449 (82.28%); 4,343 (80.28%)
Ramachandran allowed 923 (17.26%); 1,040 (19.22%)
Ramachandran outliers 25 (0.46%); 25 (0.5%)
RNA
Correct sugar puckers 99.78%; 99.42%
Correct backbone conformations 79.23%; 75.41%
Bad bonds 0/109,772; 0/109,772
Bad angles 5/171,185; 8/171,185

FSC, Fourier shell correlation; CC, correlation coefficient; RMS, root‐mean‐square.

a

Only across atoms in the model; compiled using Phenix (Afonine et al, 2013).

b

Compiled using MolProbity (Chen et al, 2010); p, percentile.

c

Clashscore is the number of serious steric overlaps (> 0.4 Å) per 1,000 atoms.