9D4D

Crystal structure of the catalytic region of human MASP-2 with specific inhibitor Compound S3

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	2023-12-01
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.95358
Spacegroup name	C 1 2 1
Unit cell lengths	72.650, 41.110, 103.130
Unit cell angles	90.00, 98.22, 90.00

Refinement procedure

Resolution	35.950 - 2.360
Rwork	0.200
R-free	0.25090
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]	35.950	2.440
High resolution limit [Å]	2.360	2.360
Rmerge	0.185	1.655
Number of reflections	12638	1256
<I/σ(I)>	5.88	0.92
Completeness [%]	99.7
Redundancy	3.7
CC(1/2)	0.988	0.281

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	2.0 uL of protein (0.62 mg/mL MASP2) was mixed with 2.0 uL of reservoir solution (0.1 M Tris-HCl pH 7.6, 0.16 M NaCl, 30% (w/v) PEG 6000, 10% (v/v) glycerol) and equilibrated against reservoir at 20 C. Crystals were soaked in reservoir supplemented with 20% (v/v) glycerol and 0.5 mM Compound S3.