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. 2020 Oct 19;40(1):e105907. doi: 10.15252/embj.2020105907

Table 1.

Cryo‐EM data collection, refinement and validation statistics

H2A.B‐NCP (EMD‐30078) (PDB 6M4H) Pb‐H2A.B‐NCP C1 symmetry Pb‐H2A.B‐NCP C2 symmetry (EMD‐30077) (PDB 6M4G) Pb‐H2A.B‐NCP Class 2 H2A.Z.2.2‐NCP (EMD‐30076) (PDB 6M4D)
Data collection and processing
Microscope Titan Krios Titan Krios Titan Krios Titan Krios Titan Krios
Camera K2 Summit K2 Summit K2 Summit K2 Summit K2 Summit
Magnification 130,000 130,000 130,000 130,000 130,000
Voltage (kV) 300 300 300 300 300
Pixel size (Å) 1.04 1.04 1.04 1.04 1.04
Electron exposure (e2) 50 50 50 50 50
Exposure per frame (e2) 1.35 1.35 1.35 1.35 1.5
Number of frames collected 37 37 37 37 32
Defocus range (μm) −0.4 to −1.0 −0.4 to −1.0 −0.4 to −1.0 −0.4 to −1.0 −2.0 to −3.0
Phase shift (π) 0.2 to 0.8 0.2 to 0.8 0.2 to 0.8 0.2 to 0.8
Symmetry imposed C2 C1 C2 C1 C2
Micrographs recorded/used (no.) 1,918/1,700 3,130/2,086 3,130/2,086 3,130/2,086 1,201/1,020
Initial particle images (no.) 141,738 416,922 416,922 416,922 181,600
Final particle images (no.) 38,472 110,355 62,980 77,017 111,800
Final reconstruction package cryoSPARC cisTEM cisTEM RELION‐3.0 RELION‐3.0
Map resolution (Å) 3.9 3.2 2.8 6.2 4.4
FSC threshold 0.143 0.143 0.143 0.143 0.143
Refinement
Initial model used (PDB) 2CV5 2CV5 1F66
Model composition
Non‐hydrogen atoms 9,420 9,032 10,303
Protein residues 656 657 682
Ligands 0.00 0.00 0.00
Validation
MolProbity score 1.86 1.42 2.17
Clashscore 12.21 5.11 21.88
Poor rotamers (%) 0 0.71 0.00
Ramachandran plot
Favored (%) 97.19 97.19 95.20
Allowed (%) 2.81 2.81 3.00
Disallowed (%) 0.00 0.00 1.80