Table 1.

Overview of Cryo-EM data collection and coordinate refinement.

	Apo hMRP4	PGE1-bound hMRP4	ATP-bound hMRP4	Sulindac-bound hMRP4
Data collection and processing
Magnification	105,000×	105,000×	105,000×	96,000×
Voltage (kV)	300	300	300	300
Camera	Gatan K3 Summit	Gatan K3 Summit	Gatan K3 Summit	Falcon4
Camera mode	Super-resolution	Super-resolution	Super-resolution	Super-resolution
Electron exposure (e–/Å2)	50	50	50	50
Defocus range (μm)	0.8–1.2	0.8–1.2	0.8–1.2	0.8–1.2
Pixel size (Å)	0.856	0.855	0.855	0.86
Symmetry imposed	C1	C1	C1	C1
Initial particle projections (no.)	1,854,905	2,147,528	389,704	371,999
Final particle projections (no.)	203, 347	378, 698	108,200	151,694
Map resolution (Å)	3.13	2.95	3.48	3.77
FSC threshold	0.143	0.143	0.143	0.143
Map resolution range (Å)	2.7–10	2.5– 8.5	2.3–9.7	1.95–9.45
Refinement
Initial model used	Not applicable (N/A)	Not applicable (N/A)	Not applicable (N/A)	Not applicable (N/A)
Model resolution (Å)	3.13	2.95	3.48	3.77
FSC threshold	0.143	0.143	0.143	0.143
Map sharpening B factor (Å2)	−113.8	−133.8	−105.8	−144.2
Model composition
Non-hydrogen atoms	9969	9917	10027	9858
Protein residues	1251	1301	1251	1237
Ligand		XPG	ATP MG	SUZ
R.m.s. deviations
Bond lengths (Å)	0.011	0.011	0.012	0.005
Bond angles (°)	0.894	0.884	0.889	0.585
Validation
MolProbity score	2.22	2.111	2.08	2.13
Clashscore	6	7	5	7
Rotamer outliers (%)	0.00	0.00	0.00	0.00
Ramachandran plot
Favored (%)	98	98	98	95
Allowed (%)	2	2	2	5
Disallowed (%)	0.00	0.00	0.00	0.00