cryo-em data collection, refinement and validation statistics (17)

elife-33660-v2.xml

10.7554/eLife.33660.007

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

	mouse Piezo1 (EMDB-7042) (PDB 6B3R)
Data collection and processing
Magnification	22,500
Voltage (kV)	300
Electron exposure (e^–/Å²)	47
Defocus range (μm)	1.0–2.4
Pixel size (Å)	1.3
Symmetry imposed	C1
Initial particle images (no.)	1
Final particle images (no.)	50
Map resolution (Å) FSC threshold	3.8 0.143
Map resolution range (Å)	3.2–10.7
Refinement
Initial model used (PDB code)	4RAX
Map sharpening B factor (Å²)	−200
Model composition Non-hydrogen atoms Protein residues Ligands	35730 4554 0
B factors (Å²) Protein Ligand	302.4 N/A
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.006 1.032
Validation MolProbity score Clashscore Poor rotamers (%)	1.73 4.84 0.25
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	91.96 8.04 0

elife-38770-v2.xml

10.7554/eLife.38770.008

Table 2.Cryo-EM data collection, refinement and validation statistics.

	PCDH15_4EC/LHFPL5 (EMDB-7327) (PDB 6C13)	PCDH15_1EC/LHFPL5 (EMDB-7328) (PDB 6C14)
Data collection and processing
Microscope	Titan Krios with Volta phase plate	Titan Krios
Voltage (kV)	300	300
Electron exposure (e–/Å²)	27	74
Defocus range (μm)	0.3–1.3	0.7–2.2
Pixel size (Å)	1.72	1.04
Symmetry imposed	C2	C2
Initial particle images (no.)	288,273	972,563
Final particle images (no.)	16,733	78,792
Map resolution (Å) FSC threshold	11.3 0.143	4.5 0.143
Refinement
Initial model used (PDB code)	4XHZ	5B2G, 4P79, 5GJV, 6C10
Model resolution (Å) FSC threshold	13.8 0.5	6.9 0.5
Model resolution range (Å)
Model composition Non-hydrogen atoms Protein residues	8505 850	6749 862
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.003 0.72	0.006 1.25
Validation MolProbity score Clashscore Poor rotamers (%)	1.31 2.32 0.23	1.72 5.29 0.27
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	95.7 4.1 0.2	93.3 6.7 0

elife-38770-v3.xml

10.7554/eLife.38770.008

Table 2.Cryo-EM data collection, refinement and validation statistics.

	PCDH15_4EC/LHFPL5 (EMDB-7327) (PDB 6C13)	PCDH15_1EC/LHFPL5 (EMDB-7328) (PDB 6C14)
Data collection and processing
Microscope	Titan Krios with Volta phase plate	Titan Krios
Voltage (kV)	300	300
Electron exposure (e–/Å²)	27	74
Defocus range (μm)	0.3–1.3	0.7–2.2
Pixel size (Å)	1.72	1.04
Symmetry imposed	C2	C2
Initial particle images (no.)	288,273	972,563
Final particle images (no.)	16,733	78,792
Map resolution (Å) FSC threshold	11.3 0.143	4.5 0.143
Refinement
Initial model used (PDB code)	4XHZ	5B2G, 4P79, 5GJV, 6C10
Model resolution (Å) FSC threshold	13.8 0.5	6.9 0.5
Model resolution range (Å)
Model composition Non-hydrogen atoms Protein residues	8505 850	6749 862
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.003 0.72	0.006 1.25
Validation MolProbity score Clashscore Poor rotamers (%)	1.31 2.32 0.23	1.72 5.29 0.27
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	95.7 4.1 0.2	93.3 6.7 0

elife-44364-v3.xml

10.7554/eLife.44364.008

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

	nhTMEM16, DDM, +Ca²⁺ (EMDB-4588, PDB 6QM5)	nhTMEM16, DDM, -Ca²⁺ (EMDB-4589, PDB 6QM6)	nhTMEM16, 2N2, -Ca²⁺ (EMDB-4587, PDB 6QM4)
Data collection and processing
Microscope Camera Magnification	FEI Talos Arctica Gatan K2 Summit + GIF 49,407	FEI Talos Arctica Gatan K2 Summit + GIF 49,407	FEI Talos Arctica Gatan K2 Summit + GIF 49,407
Voltage (kV) Exposure time frame/total (s) Number of frames per image	200 0.15/9 60	200 0.15/9 60	200 0.15/9 60
Electron exposure (e–/Å²)	52	52	52
Defocus range (μm)	−0.5 to −2.0	−0.5 to −2.0	−0.5 to −2.0
Pixel size (Å) Box size (pixels)	1.012 220	1.012 240	1.012 240
Symmetry imposed	C2	C2	C2
Initial particle images (no.)	251,693	570,203	1,379,187
Final particle images (no.)	120,086	238,070	133,961
Map resolution (Å) 0.143 FSC threshold	3.64	3.68	3.79
Map resolution range (Å)	3.4–5.0	3.4–5.0	3.3–5.0
Refinement
Initial model used	PDB 4WIS	6QM5	6QMB
Model resolution (Å) FSC threshold	3.6	3.7	3.8
Model resolution range (Å)	15–3.6	15–3.7	15–3.8
Map sharpening B factor (Å²)	−126	−147	−150
Model composition Nonhydrogen atoms Protein residues Ligands	10874 1346 4	10852 1344 -	10578 1308 -
B factors (Å²) Protein Ligand	55.75 33.72	76.42 -	94.09 -
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.007 0.821	0.004 0.835	0.007 0.983
Validation MolProbity score Clashscore Poor rotamers (%)	1.47 4.02 0	1.42 4.35 0	1.53 4.09 0.18
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	95.92 4.08 0	96.74 3.26 0	95.17 4.83 0

elife-44365-v2.xml

10.7554/eLife.44365.012

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

	mTMEM16F dig, +Ca²⁺ (EMDB 4611, PDBID 6QP6)	mTMEM16F dig, -Ca²⁺ (EMDB 4612, PDBID 6QPB)	mTMEM16F 2N2, +Ca²⁺ (EMDB 4613, PDBID 6QPC)	mTMEM16F 2N2, -Ca²⁺ (EMDB 4614, PDBID 6QPI)
Data collection and processing
Microscope Camera Magnification	FEI Talos Arctica Gatan K2 Summit + GIF 49,407	FEI Talos Arctica Gatan K2 Summit + GIF 49,407	FEI Talos Arctica Gatan K2 Summit + GIF 49,407	FEI Talos Arctica Gatan K2 Summit + GIF 49,407
Voltage (kV) Exposure time frame/total (s) Number of frames per image	200 0.15/9 60	200 0.15/9 60	200 0.15/9 60	200 0.15/9 60
Electron exposure (e–/Å²)	52	52	52	52
Defocus range (μm)	−0.5 to −2.0	−0.5 to −2.0	−0.5 to −2.0	−0.5 to −2.0
Pixel size (Å) Box size (pixels)	1.012 220	1.012 220	1.012 256	1.012 220
Symmetry imposed	C2	C2	C2	C2
Initial particle images (no.)	1,348,247	1,314,676	1,019,012	1,593,115
Final particle images (no.)	219,302	194,284	186,487	280,891
Map resolution (Å) 0.143 FSC threshold	3.18	3.64	3.54	3.27
Map resolution range (Å)	2.9–4.5	3.2–5	3.3–5	3.0–4.2

Refinement
Initial model used	PDBID 5OYB	PDBID 6QP6	PDBID 6QP6	PDBID 6QPB
Model resolution (Å) FSC threshold	3.3	3.8	4.0	7.0
Model resolution range (Å)	80–3.2	80–3.6	80–3.5	80–3.3
Map sharpening B factor (Å²)	−94	−139	−121	−131
Model composition Nonhydrogen atoms Protein residues Ligands	12144 1462 8	12136 1460 2	9060 1138 6	2288 462 -
B factors (Å²) Protein Ligand	53.3 39.1	52 34.8	72.7 54.6	7.8 -
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.009 1	0.007 0.9	0.005 0.87	0.004 0.655
Validation MolProbity score Clashscore Poor rotamers (%)	1.36 6.5 0.46	1.23 4.5 0.3	1.3 5.6 0.22	1.17 2.4 0
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	98.6 1.4 0	98.4 1.6 0	98.4 1.6 0	97.2 2.8 0

elife-45185-v1.xml

10.7554/eLife.45185.016

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

	Structure of the 5’ ETS RNP PDB 6ND4 EMD-0441
Data collection and processing
Voltage (kV)	300
Pixel size (Å)	1.6
Electron exposure (e- / Å²)	31.25
Defocus range (um)	1–3.5
Symmetry imposed	C1
Initial particle images	275’080
Final particle images	52’629
Resolution (Å)	4.3
FSC threshold	0.143
Map sharpening B-Factor (Å² )	−64.77

Refinement
Initial model used	5WLC
Model composition
Non hydrogen atoms	64,019
Protein residues	10309
RNA bases	569
Ligands	0
R.m.s. deviations
Bond length (Å)	0.01
Angles (°)	1.25
Validation
MolProbity score	1.71
Clashscore	5.26
Poor rotamers (%)	0.0
Good sugar puckers (%)	98.7
Ramachandran
Favored (%)	93.39
Allowed (%)	6.56
Outliers (%)	0.05

elife-46986-v1.xml

10.7554/eLife.46986.012

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

	Dataset 1 Slc26a9^T in detergent (EMD-4997) (PDB 6RTC)	Dataset 2 Slc26a9^T in nanodiscs (EMD-4998) (PDB 6RTF)
Data collection and processing
Microscope	FEI Titan Krios	FEI Tecnai G² Polara
Camera	Gatan K2 Summit + GIF	Gatan K2 Summit + GIF
Magnification	6,511	37,313
Voltage (kV)	300	300
Electron exposure (e–/Å²)	70	60
Defocus range (μm)	−0.5 to −3.0	−0.5 to −3.0
Pixel size (Å)^*	1.075 (0.5375)	1.34
Symmetry imposed	C2	C2
Initial particle images (no.)	416,164	711,032
Final particle images (no.)	112,930	17,442
Map resolution (Å) FSC threshold 0.143	3.96	7.77
Map resolution range (Å)	3.0–4.2	6.0–10.0
Refinement
Model resolution (Å) FSC threshold 0.5	4.0	8.0
Model resolution range (Å)	118–3.96
Map sharpening b-factor (Å²)	−205	−512
Model composition Non-hydrogen atoms Protein residues	9570 1242	9570 1242
B factors (Å²) Protein	73	73
Refmac FSC_avg/Rfactor	0.851/0.351
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.005 0.888	0.006 1.195
Validation MolProbity score Clashscore Poor rotamers (%)	1.10 1.19 0	1.07 0.78 0
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	96.10 3.90 0	95.28 4.72 0

^*Values in parentheses indicate the pixel size in super-resolution.

elife-47746-v2.xml

10.7554/eLife.47746.008

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

	TRPV3_K169A (EMD-20192) (PDB 6OT2)	TRPV3_{K169A 2-APB} (EMD-20194) (PDB 6OT5)
Data collection and processing
Magnification	130,000x	75,000x
Voltage (kV)	300	300
Electron exposure (e–/Å²)	40	42
Defocus range (μm)	1–2.5	1.25–3
Pixel size (Å)	1.06	1.08
Symmetry imposed	C4	C4
Initial particle images (no.)	452,388	1,174,521
Final particle images (no.)	95,184	79,006
Map resolution (Å)	4.1	3.6
FSC threshold	0.143	0.143
Refinement
Initial model used (PDB code)	6MHO	6MHO
Model resolution (Å)	4.1	3.6
FSC threshold	0.143	0.143
Map sharpening B factor (Å²)	−120	−100
Model composition
Non-hydrogen atoms	17,332	17,800
Protein residues	2500	2492
Ligands	0	4 (2-APB)
B factors (Å²)
Protein	87.43	40.51
Ligand	n/a	35.66
R.m.s. deviations
Bond lengths (Å)	0.008	0.008
Bond angles (°)	0.868	0.833
MolProbity score	1.64	1.24
Clashscore	5	5
Poor rotamers (%)	0	0
Ramachandran plot
Favored (%)	92.70	97.01
Allowed (%)	7.30	2.99
Disallowed (%)	0	0

elife-53199-v2.xml

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

	Complex between COMPASS and the H2B-Ub nucleosome (EMDB-21157) (PDB 6VEN)
Data collection and processing
Magnification	81,000
Voltage (kV)	300
Electron exposure (e–/Å²)	50
Defocus range (μm)	−1.0 to −2.5
Pixel size (Å)	1.08
Symmetry imposed	C1
Initial particle images (no.)	2,036,654
Final particle images (no.)	179,588
Map resolution (Å) FSC threshold	3.37 (0.143)
Map resolution range (Å)	999–3.37
Refinement
Initial model used (PDB code)	PDB: 6NJ9, 6BX3, 6CHG
Model resolution (Å) FSC threshold	3.40 (0.5)
Model resolution range (Å)	47.6 to 3.40
Map sharpening B factor (Å²)	−122.6
Model composition Non-hydrogen atoms Protein residues Ligands	24,032 2271 2
B factors (Å²) Protein Ligand	102.57 113.31
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.004 0.696
Validation MolProbity score Clashscore Poor rotamers (%)	1.92 9.79 0.05
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	94.01 5.99 0.0

elife-53311-v2.xml

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

	TRPC6-AM-1473 EMD-20954 PDB 6UZA	TRPC6-AM-0883 EMD-20953 PDB 6UZ8
Data Collection/processing Microscope Voltage (kV) Defocus range (mM) Exposure length (s) Electron exposure (e^-/Å) Number of frames Pixel size (Å) Initial particles images (no.) Final particles images (no.) Resolution (Å) FSC threshold Symmetry imposed	Titan Krios (FEI) 300 −2.3 to −0.8 6 50 30 0.832 1,590,640 90,014 3.08 0.143 C4	Titan Krios (FEI) 300 −2.3 to −0.8 6.2 50 31 1.248 1,209,330 68,553 2.84 0.143 C4
Refinement Model composition Protein residues Ligands R.m.s. deviations Bond length (Å) Bond angle (°) Ramachandran plot Favored (%) Allowed (%) Disallowed (%) Validation MolProbity score Clashscore Poor rotamers (%) CaBLAM outliers (%) EMRinger score	2936 20 0.005 0.813 95.97 4.03 0 1.29 2.30 0 3.48 3.55	2936 16 0.005 0.823 95.56 4.44 0 1.28 1.99 0 2.51 3.29

elife-53322-v2.xml

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

	BBSome (EMD-21144) (PDB 6VBU)	BBSome:ARL6:GTP (EMD-21145) (PDB 6VBV)
Data collection and processing
Magnification	81,000	81,000
Voltage (kV)	300	300
Electron exposure (e–/Å²)	56	56
Defocus range (μm)	−1.1 to −2.4	−1.1 to −2.4
Pixel size (Å)	1.06	1.06
Symmetry imposed	C1	C1
Final particle images (no.)	152,942	75,201
Map resolution (Å) FSC threshold	3.1 0.143	3.5 0.143
Refinement
Resolution limit set in refinement (Å)	3.1	3.5
Map sharpening B factor (Å²)	−45.9	−43.6
Model composition Non-hydrogen atoms Protein residues Ligands	30,209 3820 2 Ca²⁺	31,676 4000 2 Ca²⁺; 1 GTP
B factors (Å²) Protein Ligand	60.8 74.0	53.9 82.3
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.005 0.68	0.004 0.71
Validation MolProbity score Clashscore Poor rotamers (%)	2.02 12.0 0.2	2.07 12.7 0.7
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	93.5 6.5 0.0	92.7 7.2 0.1

elife-54670-v2.xml

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

	frPanx- ΔLC (EMD-21150) (PDB: 6VD7)
Data collection and processing
Magnification	130,000
Voltage (kV)	300
Electron exposure (e–/Å²)	57.2
Defocus range (μm)	1.2–2.8
Pixel size (Å)	1.07
Symmetry imposed	C7
Initial particle images (no.)	297374
Final particle images (no.)	90185
Map resolution (Å) FSC threshold	3.02 0.143
Refinement
Initial model used (PDB code)	de novo
Model resolution (Å) FSC threshold	3.29 0.5
Model resolution range (Å)	3–6
Map sharpening B factor (Å²)	−90
Model composition Non-hydrogen atoms Protein residues Ligands	16506 2079 0
CC map vs. model (%)	0.85
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.008 0.759
Validation MolProbity score Clashscore Poor rotamers (%)	1.92 5.96 0.78
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	88.32 11.68 0

elife-55015-v2.xml

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

Data collection and processing
Magnification	29,000
Voltage (kV)	300
Electron exposure (e^-/Å²)	98
Defocus range (μm)	0.5–2.0
Pixel size (Å)	1.00
Symmetry imposed	C1
No. Initial particle images	437,872
No. Final particle images	110,105
Map resolution (Å)	3.6
FSC threshold	0.143
Map resolution range (Å)	3.5–4.3
Map sharpening B factor (Å²)	−126
Refinement
Initial model used (PDB code)	6IW3
Model resolution (Å)	3.5
FSC threshold	0.5
Model composition
Chains	12
Non-hydrogen atoms	7572
Protein residues	936
B factors (Å²)	59.4
R.m.s. deviations
Bond lengths (Å)	0.004
Bond angles (°)	0.65
Validation
MolProbity score	1.47
Clashscore	4.58
Poor rotamers (%)	0.00
Ramachandran plot
Favored (%)	96.4
Allowed (%)	3.6
Disallowed (%)	0

elife-56178-v2.xml

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

	Nucleosome-CHD4 complex (EMD-10058) (PDB 6RYR)	Nucleosome-CHD4₂ complex (EMDB-10059) (PDB 6RYU)
Data collection and processing
Magnification	130,000	130,000
Voltage (kV)	300	300
Electron exposure (e–/Å²)	43–45	43–45
Defocus range (μm)	0.25–4	0.25–4
Pixel size (Å)	1.05	1.05
Symmetry imposed	C1	C1
Initial particle images (no.)	650,599	650,599
Final particle images (no.)	89,623	40,233
Map resolution (Å) FSC threshold	3.1 0.143	4.0 0.143
Map resolution range (Å)	3.0–5	3.7–8.3
Refinement
Initial models used (PDB code)	3LZ0, 5O9G, 2L75, 4O9I, 6Q3M	3LZ0, 5O9G, 2L75, 4O9I, 6Q3M
Map sharpening B factor (Å²)	−36	−86
Model composition Non-hydrogen atoms Protein residues Nucleotides Ligands	17,834 1463 298 4	23,598 2180 298 8
B factors (Å²) Protein Nucleotide Ligand	45.28 71.82 60.10	95.29 112.27 125.7
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.003 0.638	0.005 1.028
Validation MolProbity score Clashscore Poor rotamers (%)	1.54 5.69 0.08	1.92 6.52 1.64
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	96.50 3.50 0.0	94.16 5.84 0.0

elife-56185-v1.xml

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

	Wild type (EMDB-10429) (PDB 6TAX)	R4753K (EMDB-10430) (PDB 6TAY)
Data collection and processing
Magnification	130kx	130kx
Voltage (kV)	300	300
Electron exposure (e–/Å²)	59.9	47.3
Defocus range (μm)	–1.5 to –3.5	–0.8 to –2.0
Pixel size (Å)	1.04	1.04
Symmetry imposed	C1	C1
Initial particle images (no.)
Final particle images (no.)	374683	426312
Map resolution (Å) FSC threshold	3.2 0.143	3.2 0.143
Map resolution range (Å)	3.1-6.5	2.9-6.5
Refinement
Initial model used (PDB code)	none	none
Model resolution (Å) FSC threshold	3.3 0.5	3.3 0.5
Model resolution range (Å)	3.1-6.5	2.9-6.5
Map sharpening B factor (Å²)	–50	–50
Model composition Non-hydrogen atoms Protein residues Ligands	35241 4383 ATP, Zn, Mg	35235 4382 ATP, Zn, Mg
B factors (Å²) Protein Ligand (ATP)	86 64	64 50
R.m.s. deviations Bond lengths (Å) Bond angles (°)	0.011 1.17	0.007 1.01
Validation MolProbity score Clashscore Poor rotamers (%)	1.9 5.9 0.5	1.7 4.6 0.2
Ramachandran plot Favored (%) Allowed (%) Disallowed (%)	90.1 9.8 0.2	91.8 8.2 0.1

elife-56664-v1.xml

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

Data Collection and processing
Microscope	Titan krios, (UCSF)
Camera	K3
Magnification	60,010
Voltage (kV)	300 kV
Electron exposure (e^-/Å²)	86.4
Defocus range (µm)	−0.5 to −2.0
Pixel size (Å)	0.8332
Software	SerialEM
Reconstruction	CI* Peripheral Arm	CI* Membrane Arm	CI* Composite Map
Number of particles	34,407	34,407	The CI* Peripheral Arm and Membrane Arm Maps were combined in Phenix to generate this composite map
Accuracy of rotations (°)	0.68	1.489
Accuracy of translations (pixels)	0.655	0.881
Box size (pixels)	512	512
Final resolution (Å)	3.8	3.9
Map sharpening B factor (Å²)	−90	−96
EMDB ID	22093	22092	22090
Refinement
Software	Phenix
Initial model (PDB code)	6Q9D	6Q9B and 1QRG	6Q9D, 6Q9B and 1QRG
Map/model correlation
Model resolution (Å)	3.9	4.0	3.9
d99 (Å)	3.9	4.0	4.0
FSC model 0.5 (Å)	3.9	3.9	3.9
Map CC (around atoms)	0.82	0.86	0.87
Model composition
Non-hydrogen atoms	26,001	19,052	45047
Protein residues	3284	2453	5736
Number of chains	17	18	34
Number of ligands and cofactors	11	1	12
Number of lipids	0	6	6
Atomic Displacement Parameters (ADP)
Protein average (Å²)	68.78	58.40	64.39
Ligand average (Å²)	48.59	48.59	48.59
R.m.s. deviations
Bond lengths (Å)	0.007	0.007	0.007
Bond angles (°)	1.187	1.122	0.845
Ramachandran Plot
Favored (%)	82.90	88.03	84.98
Allowed (%)	16.76	11.88	14.79
Disallowed (%)	0.34	0.08	0.23
Validation
MolProbity score	2.41	2.31	2.38
Clash score	16.79	16.21	16.42
Rotamer outliers (%)	0.25	0.20	0.23
EMRinger score	1.47	2.09	2.17
PDB ID	---	---	6X89

elife-59407-v2.xml

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

Data collection and processing
Magnification	105000
Voltage (kV)	300
Electron exposure (e^-/Å²)	85
Defocus range (μm)	0.6–2.3
Pixel size (Å)	0.84
Symmetry imposed	C1
Initial particle images (no.)	889272
Final particle images (no.)	285688
Map resolution (Å)	2.98
FSC threshold	0.143
Map resolution range (Å)	2.85–4.2
Refinement	Monomer	Dimer
Initial model used (PDB code)	6CFW, 4HEA	6CFW, 4HEA
Model resolution (Å)	2.97	3.04
FSC threshold	0.5	0.5
Map sharpening B factor (Å)	−42, local resolution-filtered	−42
Model composition
Non-hydrogen atoms	15448	30250
Protein residues	1873	3730
Ligands	510	1020
Waters	242	0
B factors (Å²)
Protein	88.4	74.4
Ligand	139.1	123.4
Waters	89.8	N/A
R.m.s. deviations
Bond lengths (Å)	0.0080	0.0078
Bond angles (°)	1.32	1.33
Validation
MolProbity score	1.47	1.31
Clashscore	3.58	2.17
Poor rotamers (%)	0.13	0.10
Ramachandran plot
Favoured (%)	95.44	95.45
Allowed (%)	4.56	4.55
Disallowed (%)	0	0
EMRinger score	3.73	3.61