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. Author manuscript; available in PMC: 2024 Jun 1.
Published in final edited form as: Nat Struct Mol Biol. 2023 May 25;30(6):824–833. doi: 10.1038/s41594-023-00991-z

Table 1.

Cryo-EM data collection, refinement, and validation statistics

CLP1-TSEN(AAA)-tRNA-Arg (EMDB-26856) (7UXA) TSEN(WT)-2’F-tRNA-Arg (EMDB-28755)
Data collection and processing
Magnification 45000x 81000x 81000x
Voltage (kV) 200 300 300
Electron exposure (e–/Å2) 54 60 60
Defocus range (μm) −0.8 to −1.8 −1.2 to 2.2 −1.2 to 2.2
Pixel size (Å) 0.93 0.53 0.53
Symmetry imposed C1 C1
Initial particle images (no.) 570,104 1,557,097
Final particle images (no.) 153,031 161,512
Map resolution (Å) 3.32 3.93
 FSC threshold 0.143 0.143
Map resolution range (Å) 2.8–50.8 3.24–60.53
Refinement
Initial model used (PDB code) 6Z9U, 3L0U
Model resolution (Å) 3.25
 FSC threshold 0.143
Model resolution range (Å) 3.2–3.4
Map sharpening B factor (Å2) 121.9
Model composition
 Non-hydrogen atoms 8120
 Protein residues 820
 Nucleotides 78
 Ligands 2 (Mg)
B factors (Å2)
 Protein 76.24
 Nucleotide 81.90
 Ligand 22.87
R.m.s. deviations
 Bond lengths (Å) 0.004 (0)
 Bond angles (°) 0.832 (0)
Validation
 MolProbity score 1.77
 Clashscore 7.47
 Poor rotamers (%) 0.88
Ramachandran plot
 Favored (%) 94.78
 Allowed (%) 5.22
 Disallowed (%) 0.00