1MD7

Monomeric structure of the zymogen of complement protease C1r

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID13
Synchrotron site	ESRF
Beamline	ID13
Temperature [K]	77
Detector technology	CCD
Collection date	2000-10-28
Detector	MARRESEARCH
Wavelength(s)	0.964
Spacegroup name	P 64
Unit cell lengths	167.060, 167.060, 43.648
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 3.200
R-factor	0.2428
Rwork	0.217
R-free	0.27860 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007 *
RMSD bond angle	25.000 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	3.370
High resolution limit [Å]	3.200	3.200
Rmerge	0.120 *	0.360 *
Number of reflections	48443 *
<I/σ(I)>	5	1.8
Completeness [%]	95.9 *	95.3
Redundancy	4.4	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4 *	293	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	drop	protein	8 (mg/ml)
2	1	drop	triethanolamine-hydrochloride	50 (mM)
3	1	drop		145 (mM)	pH7.4
4	1	reservoir	ammonium sulfate	1.5 (M)
5	1	reservoir	TAPS	100 (mM)	pH8.4