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. 2023 Aug 31;30(10):1481–1494. doi: 10.1038/s41594-023-01080-x

Table 2.

Cryo-EM data collection, refinement and validation statistics

GluA2–γ5–CNIH2ZK-PMP-SPD
LBD–TMD
(EMDB-40746)
(PDB 8SS7)
GluA2–γ5ZK-PMP
FL
(EMDB-40747)
(PDB 8SS8)
GluA2–γ5ZK-PMP
LBD–TMD
(EMDB-40748)
(PDB 8SS9)
GluA2–γ5–CNIH2Glu-SPD
FL
(EMDB-40749)
(PDB 8SSA)
GluA2–γ5–CNIH2Glu-SPD
LBD–TMD
(EMDB-40750)
(PDB 8SSB)
Data collection and processing
Magnification ×75,000 ×75,000 ×75,000 ×105,000 ×105,000
Voltage (kV) 300 300 300 300 300
Electron exposure (e2) 50 50 50 58 58
Defocus range (μm) −1 to −2 −1 to −2 −1 to −2 −1 to −2 −1 to −2
Pixel size (Å) 0.925 0.925 0.925 0.83 0.83
Symmetry imposed C2 C2 C2 C2 C2
Initial particle images (no.) 2,360,956 2,360,956 2,360,956 2,282,408 2,282,408
Final particle images (no.) 126,263 126,964 117,939 58,186 48,434
Map resolution (Å) 2.76 2.81 2.72 3.88 3.66
FSC threshold 0.143 0.143 0.143 0.143 0.143
Map resolution range (Å) 2.6/3.3/34.4 2.0/3.3/36.3 2.0/3.3/36.0 2.1/5.8/42.5 2.1/4.8/36.5
Refinement
Initial model used (PDB code) 7RZ5, 7OCE 7RZ5, 7OCE 7RZ5, 7OCE 7RZ5, 7OCE 7RZ5, 7OCE
Model resolution (Å) 2.76 2.81 2.72 3.88 3.66
FSC threshold
Map sharpening B factor (Å2) −132.7 −135.5 −131.4 −101.4 −97.2
Model composition
Nonhydrogen atoms 19,436 28,487 16,319 30,888 19,048
Protein residues 2,266 3,514 1,986 3,840 2,304
Ligands
PMP 4 4 4
SPD 1 1 1
ZK 4 4 4
Glutamate (Glu) 4 4
B factors (Å2)
Protein 63.09 68.50 65.55 128.43 68.50
Ligand 41.07 98.06 65.93 66.30 98.06
R.m.s. deviations
Bond lengths (Å) 0.010 0.014 0.008 0.010 0.007
Bond angles (°) 1.657 1.585 1.541 1.431 1.376
Validation
MolProbity score 1.92 1.75 1.51 1.96 2.01
Clashscore 6.95 3.86 4.43 6.33 7.27
Poor rotamers (%) 1.45 1.33 0.36 1.00 0.72
Ramachandran plot
Favored (%) 93.80 92.19 95.80 87.63 87.37
Allowed (%) 5.66 7.12 3.89 11.37 11.40
Disallowed (%) 0.54 0.69 0.31 1.00 1.24