9D40

Crystal structure of the catalytic region of human MASP-2 with specific inhibitor Analog 20

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	72.520, 40.980, 101.870
Unit cell angles	90.00, 97.82, 90.00

Refinement procedure

Resolution	20.490 - 1.760
R-factor	0.2005
Rwork	0.198
R-free	0.25380
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]	20.490	1.823
High resolution limit [Å]	1.760	1.760
Rmerge	0.109	1.598
Number of reflections	29662	11111
<I/σ(I)>	7.13	0.89
Completeness [%]	99.7
Redundancy	3.7
CC(1/2)	0.996	0.339

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 Analog 20) and equilibrated against reservoir at 20 C. Crystals were cryoprotected in reservoir supplemented with 20% (v/v) glycerol.