1ELV

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	1998-09-24
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	39.080, 79.650, 60.210
Unit cell angles	90.00, 91.24, 90.00

Refinement procedure

Resolution	15.000 - 1.700
R-factor	0.185 *
Rwork	0.186
R-free	0.21900
RMSD bond length	0.020
RMSD bond angle	0.024
Data reduction software	XDS
Data scaling software	XDS
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.750
High resolution limit [Å]	1.700	1.700
Rmerge	0.037 *	0.247 *
Total number of observations	115710 *
Number of reflections	39489 *
<I/σ(I)>	16.9	3.4
Completeness [%]	93.0	75.8
Redundancy	2.9	1.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.4	4 *	PEG 4K 34%, AMMONIUM SULFATE 100mM, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	drop	TEA-HCl	50 (mM)
3	1	drop		145 (mM)
4	1	reservoir	PEG4000	34 (%)
5	1	reservoir	ammonium sulfate	100 (mM)