Table 1.

Cryo-EM data collection, refinement and validation statistics

	ScElongator EMD-15622 PDB ID 8ASV	ScElp456 EMD-15635 PDB ID 8AT6	ScElp123–tRNA EMD-15623 PDB ID 8ASW	MmElp123 EMD-15682 PDB ID 8AVG	MmElp123–tRNA EMD-15625	MmElongator EMD-15626
Data collection and processing
Magnification	105 000×	81 000×	165 000×	105 000×	105 000×	105 000×
Voltage (keV)	300	300	300	300	300	300
Electron exposure (e-/Å2)	40	40	42.45	40	40	40
Defocus range	−0.9 to −3.0	−0.9 to −3.0	−0.8 to −2.0	−0.9 to −3.0	−0.9 to −1.5	−0.9 to −3.0
Pixel size (Å)	0.86	1.1	0.81	0.86	0.86	0.86
Symmetry imposed	C1	C1	C1	C1	C1	C1
Initial particle images (no.)	188 389	364 424	693 585	364 424	161 871	581 666
Final particle images (no.)	12 514	128 593	16 809	42 894	24 829	27 128
Map resolution (Å)	4.35	3.7	3.96	4.01	4.35	5.9
FSC threshold	0.143	0.143	0.143	0.143	0.143	0.143
Map resolution range (Å)	3.9 to >10	3.6 to 6.6	3.7 to 9.7	3.8 to >10	2.8 to >10	4.4 to >10
Refinement
Initial model used	6QK7 and 4A8J	4A8J	6QK7	6QK7
Model resolution (Å)	3.5	3.7	3.5	3.5
FSC threshold	0.143	0.143	0.143	0.143
Model resolution range (Å)	n/a	n/a	n/a	n/a
Map sharpening B factor (Å2)	−141.69	−129.16	−67.83	−131.78
Model composition
Non-hydrogen atoms	35 795	12 587	24 783	13 749
Protein residues	4478	1580	2897	1732
Nucleotide residues			73
Ligands	1	0	2	2
B factors (Å2)
Protein	99.05	107.76	97.38	84.42
Nucleotide			254.23
Ligands	60.85		61.57	55.04
R.m.s. deviations
Bond lengths (Å)	0.004	0.004	0.006	0.004
Bond angles (°)	0.990	0.974	1.014	0.989
Validation
MolProbity score	2.13	1.92	2.35	2.17
Clashscore	12.59	9.75	19.37	13.21
Poor rotamers (%)	0.02	0.00	0.71	0.07
Ramachandran
Favored (%)	90.93	93.80	89.25	90.48
Allowed (%)	9.00	5.88	10.51	9.34
Disallowed (%)	0.07	0.32	0.24	0.18
CC volume	0.65	0.85	0.76	0.71