Table 1 Cryo-EM map and model statistics

From: Real-time capture of σ^N transcription initiation intermediates reveals mechanism of ATPase-driven activation by limited unfolding

Complex	RPi1^open (open ring)	RPi1^closed (closed ring)	RII	RPo	RPo+2A
PDB ID	9MSE	9MSF	9MSG	9MSH	9MSJ
EMDB ID	EMD-48586 EMD-48580 EMD-48581 EMD-48582	EMD-48587 EMD-48583 EMD-48584 EMD-48585	EMD-48588	EMD-48589 EMD-48576 EMD-48577	EMD-48590 EMD-48578 EMD-48579
Data collection
Camera	Gatan K3
Dose rate (e⁻/Å²/s)	30
Electron exposure (e⁻/Å²)	42
Defocus range (μm)	−0.8 to −2.2
Pixel size (Å)	0.86
Energy filter slit width (eV)	20
Cs (mm)	0.001
Images collected	17,199
Symmetry imposed	C1
Initial particles	2,798,596
Consensus final particles	1,060,259
Consensus resolution (Å)^a	2.3
Processing statistics
Class particles	118,561	260,106	95,920	45,631	15,649
bEBP map resolution (Å)^a	3.1 Å	3.0 Å	n/a	n/a	n/a
Sharpening b-factor	−85.4	−95.2	n/a	n/a	n/a
RNAP map resolution (Å)^a	2.7 Å	2.6 Å	2.7 Å	2.8 Å	3.1 Å
Sharpening b-factor	−61.6	−68.1	−60.4	−54.1	−39.4
σ^N map resolution (Å)^a	3.1 Å	3.0 Å	n/a	3.2 Å	3.6 Å
Sharpening b-factor	−74.2	−80.3	n/a	−67.2	−55.5
Refinement
Initial models used	8F1K 4LZZ	8F1K 4LZZ	8F1K 4LZZ	8F1K 6GH5	8F1K 6GH5
Non-hydrogen atoms	43,810	44,073	42,869	31,061	31,102
Protein residues	5200	5201	5235	3664	3687
Nucleotides	92	92	68	98	104
Water molecules	703	986	29	348	54
Ligands	12	11	11	4	5
RMS (bonds)	0.003	0.002	0.002	0.003	0.003
RMS (angles)	0.458	0.446	0.459	0.515	0.505
Ramachandran favored	97.75 %	98.18 %	97.73 %	97.20 %	98.42 %
Ramachandran allowed	2.23 %	1.82 %	2.27 %	2.80 %	1.58 %
Ramachandran outliers	0.02 %	0.00 %	0.00 %	0.00 %	0.00 %
Rotamer outliers	1.10 %	1.12 %	1.56 %	2.74 %	2.44 %
Clashscore	3.36	3.62	4.72	4.62	4.64
MolProbity score	1.21	1.19	1.45	1.72	1.53

^a FSC threshold 0.143.
Calculation of model statistics was performed using MolProbity.

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