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. 2021 Dec 1;7(49):eabl3857. doi: 10.1126/sciadv.abl3857

Table 1. Cryo-EM data collection, refinement, and validation statistics.

5-HT–SERT
outward-NaCl
(EMD-23365)
(PDB 7LIA )
5-HT–SERT
occluded-NaCl
(EMD-23830)
(PDB 7MGW)
5-HT–SERT
inward-KCl
(EMD-23364)
(PDB 7LI9)
Apo SERT
occluded-NaCl
(EMD-23362)
(PDB 7LI7)
Apo SERT
inward-NaCl
(EMD-23363)
(PDB 7LI8)
Apo SERT
inward-KCl
(EMD-23361)
(PDB 7LI6)
Data collection and processing
  Magnification 77,160 62,383 77,160 75,642
  Voltage (kV) 300 300 300 300
  Electron exposure
(e−/Å2)
55 57 50 52
  Defocus range (μm) −0.8 to −2.5 −0.9 to −2.7 −1.0 to −2.5 −1.0 to −2.5
  Pixel size (Å) 0.648 0.802 0.648 0.661
  Symmetry imposed C1 C1 C1 C1 C1 C1
  Initial particle images
(no.)
2,861,741 5,624,930 5,568,431 5,865,511
  Final particle images
(no.)
774,907 114,222 299,808 636,335 343,085 707,210
  Map resolution (Å) 3.1 3.5 3.7 3.9 3.9 3.5
  FSC threshold 0.143 0.143 0.143 0.143 0.143 0.143
  Map resolution range (Å) 3.4–2.6 3.8–3.0 4.0–3.0 4.0–3.2 4.2–3.4 3.6–3.0
Refinement
  Initial model used
(PDB code)
6DZW 6DZV 6DZZ 6DZV 6DZZ 6DZZ
  Initial model CC 0.59 0.78 0.83 0.56 0.74 0.64
  Model resolution (Å) 3.5 4.0 3.9 4.1 4.2 3.8
  FSC threshold 0.5 0.5 0.5 0.5 0.5 0.5
  Map sharpening
B factor (Å2)
−178 −157 −161 −214 −195 −185
Model composition
  Nonhydrogen atoms 6,279 6,223 6,174 6,177 6,181 6,249
  Protein residues 767 765 767 765 767 767
  Ligands (atoms) 231 188 128 142 137 224
B factors (Å2)
  Protein 28 192 29 98 99 73
  Ligand 28 180 22 89 91 76
Root mean square deviations
  Bond lengths (Å) 0.002 0.002 0.002 0.002 0.002 0.002
  Bond angles (°) 0.422 0.470 0.444 0.470 0.461 0.444
Validation
  Refined model CC 0.72 0.84 0.71 0.67 0.79 0.71
  MolProbity score 1.71 1.75 1.70 1.81 1.74 1.81
  Clashscore 7.98 8.97 6.00 10.00 6.76 5.29
  Poor rotamers (%) 1.71 1.40 0.00 0.00 0.00 1.72
Ramachandran plot
  Favored (%) 97.50 97.10 94.61 95.78 94.74 95.01
  Allowed (%) 2.50 2.90 5.39 4.22 5.26 4.99
  Disallowed (%) 0 0 0 0 0 0