. Author manuscript; available in PMC: 2019 Jan 2.

Published in final edited form as: Nat Struct Mol Biol. 2018 Jul 2;25(7):583–590. doi: 10.1038/s41594-018-0086-9

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

	(EMDB-4173) (PDB 6f2e)
Data collection and processing
Magnification	165000 (K2), 96000 (Falcon3)
Voltage (kV)	300
Electron exposure (e–/Å²)	47 (K2), 50 (Falcon3)
Defocus range (μm)	0.5-4
Pixel size (Å)	0.86
Symmetry imposed	C1
Initial particle images (no.)	474625
Final particle images (no.)	97718
Map resolution (Å)	4.2
FSC threshold	0.143

Refinement
Initial model used (PDB code)	None
Model resolution (Å)	4.2
FSC threshold	0.143
Map sharpening B factor (Å²)	-227
Model composition
Non-hydrogen atoms	12541
Protein residues	1629
Ligands	0
B factors (Å²)
Protein	227
Ligand	0
R.m.s. deviations
Bond lengths (Å)	0.01
Bond angles (°)	1.18
Validation
MolProbity score	2.6
Clashscore	25.7
Poor rotamers (%)	0.1
Ramachandran plot
Favored (%)	83.0
Allowed (%)	16.3
Disallowed (%)	0.7