Table 2.

The statistics of cryo-EM data collection, structure refinement, and validation for the apo-AsfvTop2 structure in three states, containing six conformers

apo-AsfvTop2
Data collection and processing
Micrographs	8900
Magnification	105,000
Voltage (kV)	300
Electron exposure (e–/Å2)	50
Defocus range (μm)	−1.5 ~-2.5
Pixel size (Å)	0.83
Symmetry imposed	C2
Initial particle images (no.)	3,260,785
Conformer	Ia	Ib	IIa	IIb	IIIa	IIIb
PDB/EMDB code	8J87/EMD-36062	8J88/EMD-36063	8J89/EMD-36064	8J8A/EMD-36065	8J8B/EMD-36066	8J8C/EMD-36067
Final particle images (no.)	79,500	75,839	567,069	393,995	341,283	180,474
Map resolution (Å)	3.42	3.49	2.31	2.51	2.43	2.69
FSC threshold	0.143	0.143	0.143	0.143	0.143	0.143
Map resolution range (Å)	3.0–15.0	3.0–15.0	2.0–8.0	2.0–9.0	2.0–8.0	2.0–10.0
Refinement
Initial model used (PDB code)	1ZVU47	Ia(8J87)	Robetta prediction81	IIa(8J89)	IIa(8J89)	IIIa(8J8B)
Model resolution (Å)	3.42	3.49	2.31	2.51	2.43	2.69
Model resolution range (Å)	3.0–15.0	3.0–15.0	2.0–8.0	2.0–9.0	2.0–8.0	2.0–10.0
Map sharpening B factor (Å2)	−96.5	−111.5	−80.8	−86.7	−79.7	−79.7
Model composition
Protein residues	954	954	1502	1502	1518	1434
Non-hydrogen atoms	7846	7846	12,222	12,222	12,330	11,650
Ligand	0	0	0	0	0	0
B factors (Å2)
Protein	157.69	194.85	96.39	110.18	109.82	104.39
R.m.s. deviations
Bond lengths (Å)	0.002	0.002	0.002	0.003	0.002	0.002
Bond angles (°)	0.562	0.562	0.457	0.498	0.432	0.432
Validation
MolProbity score	1.66	1.64	1.56	1.41	1.50	1.54
Clash score	7.20	5.61	5.77	7.45	5.43	4.89
Poor rotamers (%)	0.00	0.00	0.00	0.00	0.00	0.00
Ramachandran plot (%)
Favored	96.11	95.16	96.39	97.99	96.49	95.91
Allowed	3.89	4.84	3.61	2.01	3.51	4.09
Disallowed	0.0	0.0	0.00	0.00	0.00	0.00