3GOV

Crystal structure of the catalytic region of human MASP-1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-11-01
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.8148
Spacegroup name	P 21 21 21
Unit cell lengths	68.418, 70.412, 121.413
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.980 - 2.550
R-factor	0.231
Rwork	0.229
R-free	0.27800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MASP-1 serine protease domain(unpublished) CCP1 and CCP2 modules of PDB entry 1zjk
RMSD bond length	0.007
RMSD bond angle	1.163
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.980	2.600
High resolution limit [Å]	2.550	2.550
Rmerge	0.095	0.472
Number of reflections	19349	1066
<I/σ(I)>	15.96	4.3
Completeness [%]	97.9	97.4
Redundancy	5.9	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	well solution: 11%(w/v) PEG3350, 0.1 M MES; protein solution: 50 mM NaCl, 5 mM Tris, 0.5 mM EDTA, 20 mM benzamidine-HCl, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K