Table 1.
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.
Only across atoms in the model; compiled using Phenix (Afonine et al, 2013).
Compiled using MolProbity (Chen et al, 2010); p, percentile.
Clashscore is the number of serious steric overlaps (> 0.4 Å) per 1,000 atoms.