9P1C

Crystal structure of human TMPRSS11A S368A interacting with its own zymogen activation motif

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-E
Synchrotron site	APS
Beamline	21-ID-E
Temperature [K]	100
Detector technology	PIXEL
Collection date	2025-03-21
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97920
Spacegroup name	P 41
Unit cell lengths	81.785, 81.785, 44.881
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.380 - 2.540
R-factor	0.19431
Rwork	0.192
R-free	0.24644
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.639
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.000	40.000	2.570
High resolution limit [Å]	2.530	6.860	2.530
Rmerge	0.334	0.105	1.313
Rmeas	0.368	0.115	1.571
Rpim	0.153	0.046	0.844
Total number of observations	103418
Number of reflections	9798	950	944
<I/σ(I)>	3.2
Completeness [%]	98.9	97.5	95.6
Redundancy	5.4	6.4	2.7
CC(1/2)	0.974	0.992	0.237

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4	291	1.4 M sodium/potassium phosphate pH 7.4. TMPRSS11A protein (20 mg/mL) was mixed 1:1 with precipitant (0.5 uL: 0.5 uL) using an Art Robbins Phoenix crystallization robot. Crystals were mounted with reservoir solution containing 10% ethylene glycol.