1GPZ

THE CRYSTAL STRUCTURE OF THE ZYMOGEN CATALYTIC DOMAIN OF COMPLEMENT PROTEASE C1R

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	2000-11-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	99.300, 101.800, 122.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	12.000 - 2.900
R-factor	0.242
Rwork	0.242
R-free	0.29200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1elv
RMSD bond length	0.015
RMSD bond angle	26.200 *
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.000	3.060
High resolution limit [Å]	2.900	2.900
Rmerge	0.056	0.340 *
Number of reflections	27235
<I/σ(I)>	11	2.2
Completeness [%]	99.8 *	99.8
Redundancy	5.1	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.4 *	20 *	1.5 M AMMONIUM SULFATE, 0.1M TAPS, PH 8.5, AT 20 DEG C.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2-6 (mg/ml)
2	1	drop		145 (mM)
3	1	drop	triethanolamine-hydrochloride	50 (mM)	pH7.4
4	1	reservoir	ammonium sulfate	1.5 (M)
5	1	reservoir	TAPS	100 (mM)	pH8.5