8V04

High resolution TMPRSS2 structure following acylation by nafamostat

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-03-19
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.97918
Spacegroup name	P 1 21 1
Unit cell lengths	58.757, 50.502, 64.578
Unit cell angles	90.00, 91.60, 90.00

Refinement procedure

Resolution	39.810 - 1.580
R-factor	0.15695
Rwork	0.156
R-free	0.18084
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.659
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0352)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.000	40.000	1.610
High resolution limit [Å]	1.580	4.290	1.580
Rmerge	0.099	0.047	0.663
Rmeas	0.127	0.059	0.851
Rpim	0.079	0.035	0.528
Total number of observations	212101
Number of reflections	94364	4962	4557
<I/σ(I)>	8.7
Completeness [%]	92.8	97.8	91.6
Redundancy	2.2	2.4	2.2
CC(1/2)	0.988	0.994	0.625

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	291	3 uL hanging drop (2:1 protein:precipitant) grown over precipitant solution containing 25%PEG4000, 0.2M ammonium sulfate, and 0.1M sodium acetate pH 4.6. Protein (10 mg/mL) was in a buffer containing 25 mM Tris pH 8.0, 75 mM NaCl, and 2 mM CaCl2