1MD8

Monomeric structure of the active catalytic domain of complement protease C1r

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	77
Detector technology	CCD
Collection date	2001-04-09
Detector	MARRESEARCH
Wavelength(s)	0.979549
Spacegroup name	C 1 2 1
Unit cell lengths	112.911, 49.459, 77.249
Unit cell angles	90.00, 106.19, 90.00

Refinement procedure

Resolution	50.000 * - 2.800
R-factor	0.2035
Rwork	0.198
R-free	0.25450 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	24.600 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	2.870
High resolution limit [Å]	2.800	2.800
Rmerge	0.065 *	0.189 *
Number of reflections	25998 *
<I/σ(I)>	7
Completeness [%]	98.9	99.9
Redundancy	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	20 *	ammonium sulfate, TAPS, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG6000	12-20 (%)
2	1	reservoir	HEPES	100 (mM)	pH7.5
3	1	reservoir	glycerol	20 (%)	or 5% PEG4000