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. Author manuscript; available in PMC: 2024 Apr 11.
Published in final edited form as: Nat Struct Mol Biol. 2023 Sep 7;30(10):1495–1504. doi: 10.1038/s41594-023-01085-6

Table 1 |.

Cryo-EM data collection, refinement and validation statistics

AE1-apo
(EMD-26165)
(PDB 7TY4)
AE1-bicarbonate
(EMD-26168)
(PDB 7TY7)
AE1-DIDS
(EMD-41082)
(PDB 8T6V)
AE1-H2DIDS
(EMD-26167)
(PDB 7TY6)
AE1-DEPC
(EMD-26171)
(PDB 7TYA)
AE1-dipyridamole
(EMD-41081)
(PDB 8T6U)
AE1-NIF
(EMD-26169)
(PDB 7TY8)
Data collection and processing
Magnification 64,000 64,000 81,000 64,000 81,000 64,000 64,000
Voltage (kV) 300 300 300 300 300 300 300
Electron exposure (e2) 51.85 59.99 52.09 51.85 51.18 51.69 59.99
Defocus range (μm) −0.5 to −1.8 −0.5 to −1.8 −0.5 to −1.8 −0.5 to −1.8 −0.5 to −1.8 −0.5 to −1.8 −0.5 to −1.8
Pixel size (Å) 1.076 1.076 1.083 1.076 1.083 1.076 1.076
Symmetry imposed C2 C2 C2 C2 C2 C2 C2
Initial particle images (no.) 4,357,888 2,660,401 9,728,456 2,460,255 3,156,841 4,488,247 2,977,492
Final particle images (no.) 238,474 173,471 914,784 267,008 191,625 270,791 79,981
Map resolution (Å) 2.99 3.37 2.95 2.98 3.07 3.13 3.18
 FSC threshold 0.143 0.143 0.143 0.143 0.143 0.143 0.143
Map sharpening B-factor (Å2) −150.0 −150.4 −187.0 −121.2 −128.7 −115.3 −107.4
Local resolution range (Å) 2.5–45.6 3.0–50.5 2.5–10.1 2.5–40.9 2.7–36.2 2.7–28.2 2.7–51.5
Refinement
Model composition
 Non-hydrogen atoms 8,665 8,584 8,686 8,728 8,674 8,647 8,578
 Protein residues 1,032 1,034 1,032 1,032 1,028 1,032 1,032
 Ligand 14 15 16 16 16 16 16
R.m.s. deviations
 Bond lengths (Å) 0.014 0.013 0.025 0.013 0.027 0.010 0.013
 Bond angles (°) 1.644 1.637 1.731 1.644 1.966 1.370 1.649
Validation
 Clashscore 3.32 2.71 2.36 3.03 3.28 5.69 3.10
 Poor rotamers (%) 0.49 1 0.33 1.44 0.22 0 1.89
Ramachandran plot
 Favored (%) 95.02 94.43 97.07 94.82 96.05 97.07 95.8
 Allowed (%) 4.98 5.57 2.93 5.18 3.95 2.73 4.20
 Disallowed (%) 0 0 0 0 0 0.2 0