. Author manuscript; available in PMC: 2018 Jan 6.

Published in final edited form as: Nature. 2017 Jul 6;548(7667):352–355. doi: 10.1038/nature23314

Extended Data Table 1. Statistics of the cryo-EM structures presented in this study.

Cryo-EM data collection and processing	Hrd13 dimer	Hrd1 dimer one Hrd3	Hrd1 dimer	Hrd3
Voltage (kV)	300
Electron dose (e^-/Å²)	82
Number of collected movies	5,361
Particle defocus range (average) (μm)	0.7-3.2
Number of particles for 3D classification	871,530

Number of particles for final map	139,754	167,061	93,609	204,578
Symmetry for final map	C1	C1	C2	C1
Resolution (Å)	4.7	4.7	4.1	3.9
Map sharpening B-factor (Å²)	-250	-250	-230	-290

Atomic model refinement

Number of protein residues			542	617
Number of atoms			9228	10142
Geometric parameters (r.m.s.d.)
Bond length (Å)			0.014	0.022
Bond angle (º)			1.334	1.636
Ramachandran statistics
Residues in favoured regions (%)			96.99	86.09
Residues in allowed regions (%)			2.63	13.75
Residues in disallowed regions (%)			0.38	0.16
Rotamer outliers (%)			0
MolProbity validation
Overall score			0.94	2.21
Clash score			0.87	11.34