Table 2.

Cryo-EM data collection, refinement and validation statistics

	LPAx0 (EMDB-40941) (PDB 8T0E)	LPAx1 (EMDB-40949) (PDB 8T0Y)	LPAx2 opposite (EMDB-40951) (PDB 8T10)	LPAx2 neighboring (EMDB-41005) (PDB 8T3L)	LPAx3 (EMDB-41006) (PDB 8T3M)	LPAx4 (EMDB-40940) (PDB 8T0C)
Data collection and processing
Magnification	105,000×	105,000×	105,000×	105,000×	105,000×	105,000×
Voltage (kV)	300	300	300	300	300	300
Electron exposure (e− Å−2)	45.8	45.8	45.8	45.8	45.8	45.8
Defocus range (μm)	0.5–2.0	0.5–2.0	0.5–2.0	0.5–2.0	0.5–2.0	0.5–2.0
Pixel size (Å)	0.835	0.835	0.835	0.835	0.835	0.835
Symmetry imposed	C4	C1	C2	C1	C1	C4
Initial particle images (no.)	240,263	240,263	240,263	240,263	240,263	240,263
Final particle images (no.)	4,090	7,921	2,030	7,916	10,602	11,119
Map resolution (Å)	3.3	3.5	3.7	3.6	3.5	3.5
FSC threshold	0.143	0.143	0.143	0.143	0.143	0.143
Map resolution range (Å)	3.0–19	3.4–6.8	3.7–8.6	3.6–8.0	3.5–7.8	2.8–11.9
Refinement
Initial model used (PDB code)	7L2P	7L2P	7L2P	7MZD	7MZD	7MZD
Map sharpening B factor (Å2)	NA	−76.3	−79.9	−75.1	−90.1	NA
Model composition
Nonhydrogen atoms	17,433	10,609	10,082	10,066	11,156	17,398
Protein residues	2,124	1,273	1,198	1,197	1,345	2,128
Ligands	5	5	5	6	6	6
B factors (min/max/mean Å2)
Protein	64.90/177.90/120.66	42.25/97.04/62.10	30.98/75.19/43.98	30.24/87.68/50.64	44.17/103.68/64.26	47.13/161.23/99.92
Ligand	70.00/91.19/91.00	41.82/60.80/57.59	32.54/40.27/39.83	23.02/51.00/46.32	36.62/60.92/58.30	35.05/67.49/66.40
Root mean square deviations
Bond lengths (Å)	0.37	0.32	0.46	0.32	0.34	0.28
Bond angles (°)	0.55	0.48	0.60	0.49	0.50	0.48
Validation
MolProbity score	2	1	2	1	1	1
Clashscore	5	4	4	5	7	5
Poor rotamers (%)	2	1	3	1	1	0
Ramachandran plot
Favored (%)	90	93	94	93	92	94
Allowed (%)	10	7	6	7	8	6
Disallowed (%)	0	0	0	0	0	0

NA, not applicable.