9D3Y

Crystal structure of the catalytic region of human MASP-2 with specific inhibitor Compound S2

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-11-08
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.95355
Spacegroup name	C 1 2 1
Unit cell lengths	72.770, 41.050, 102.920
Unit cell angles	90.00, 98.01, 90.00

Refinement procedure

Resolution	35.670 - 2.080
Rwork	0.207
R-free	0.26100
Structure solution method	MOLECULAR REPLACEMENT
Data reduction software	xia2
Data scaling software	xia2
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.670	2.154
High resolution limit [Å]	2.080	2.080
Rmerge	0.155	1.545
Number of reflections	18318	1815
<I/σ(I)>	6.44	1.1
Completeness [%]	99.5
Redundancy	3.7
CC(1/2)	0.993	0.348

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	1.0 uL of protein (0.62 mg/mL MASP2) was mixed with 1.0 uL of reservoir solution (0.1 M Tris-HCl pH 7.8, 0.16 M NaCl, 31% (w/v) PEG 6000, 10% (v/v) glycerol, and 200 uM Compound S2) and equilibrated against reservoir at 20 C. Crystals were cryoprotected in reservoir supplemented with 20% (v/v) glycerol.