9D17

Crystal structure of the catalytic region of human MASP-2 with specific inhibitor Compound S1

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	2023-06-23
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.95375
Spacegroup name	C 1 2 1
Unit cell lengths	71.840, 40.810, 101.500
Unit cell angles	90.00, 97.52, 90.00

Refinement procedure

Resolution	35.610 - 1.970
Rwork	0.201
R-free	0.24320
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]	35.610	2.040
High resolution limit [Å]	1.970	1.970
Rmerge	0.146	1.543
Number of reflections	20876	2068
<I/σ(I)>	6.6	1
Completeness [%]	99.7	99.76
Redundancy	3.7	3.9
CC(1/2)	0.994	0.311

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	1.5 uL of protein (0.58 mg/mL MASP2) was mixed with 1.5 uL of reservoir solution (0.1 M Tris-HCl pH 7.5, 0.2 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 1 mM Compound S1