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. Author manuscript; available in PMC: 2021 Feb 1.
Published in final edited form as: Nature. 2020 Jun 3;584(7822):646–651. doi: 10.1038/s41586-020-2357-y

Extended Data Table 3:

Cryo-EM data collection, refinement and validation statistics for N255A-hsPANX1Hemi, N255A-hsPANX1Gap, SMA-wt-hsPANX1.

PANX1(N255A)Hemi
(EMDB-21593)
(PDB 6WBM)
PANX1 (N255A)Gap
(EMDB-21594)
(PDB 6WBN)
SMA–PANX1
(EMDB-21598)

Data collection and processing
Magnification 105,000 105,000 105,000
Voltage (kV) 300 300 300
Electron exposure (e/Å2) 47.25 47.25 47.25
Defocus range (μm) −1.2 – −1.8 −1.2 – −1.8 −1.2 – −1.8
Pixel size (Å) 0.812 0.812 0.812
Symmetry imposed C7 C7 C7
Initial particle images (no.) 3,945,051 3,945,051 1,098,021
Final particle images (no.) 407,341 78,983 125,025
Map resolution (Å) 2.86 2.83 6.04
 FSC threshold 0.143 0.143 0.143
Map resolution range (Å) 2.86 – 246.2 2.83 – 246.2 6.04 – 246.2
Refinement
Initial model used (PDB code) De novo De novo
Model resolution (Å) 3.10 3.12
 FSC threshold 0.5 0.5
Model resolution range (Å)
Map sharpening B factor (Å2) −119.822 −70.501
Model composition
 Non-hydrogen atoms 19201 38402
 Protein residues 2387 4774
 Ligands 42 84
R.m.s. deviations
 Bond lengths (Å) 0.006 0.01
 Bond angles (°) 0.71 1.15
Validation
 MolProbity score 2.03 1.88
 Clashscore 13.68 11.23
 Poor rotamers (%) 0.8 0.8
Ramachandran plot
 Favored (%) 94.40 95.51
 Allowed (%) 5.60 4.49
 Disallowed (%) 0.00 0.00