9E83

TMPRSS2 crystal structure following acylation by UCSF_157

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	2022-06-11
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97918
Spacegroup name	P 1 21 1
Unit cell lengths	60.853, 51.392, 64.625
Unit cell angles	90.00, 91.01, 90.00

Refinement procedure

Resolution	39.290 - 2.070
R-factor	0.20294
Rwork	0.200
R-free	0.25991
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.501
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0352)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.000	40.000	2.100
High resolution limit [Å]	2.060	5.590	2.060
Rmerge	0.233	0.137	0.942
Rmeas	0.259	0.150	1.061
Rpim	0.110	0.061	0.476
Total number of observations	121196
Number of reflections	23755	1279	1049
<I/σ(I)>	4.1
Completeness [%]	96.3	98.5	86.1
Redundancy	5.1	5.3	4.1
CC(1/2)	0.930	0.975	0.548

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