1NZI

Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-04-21
Detector	MARRESEARCH
Wavelength(s)	0.933
Spacegroup name	P 1
Unit cell lengths	35.134, 47.499, 56.679
Unit cell angles	87.74, 78.04, 75.67

Refinement procedure

Resolution	30.000 - 1.500
R-factor	0.2173
Rwork	0.216
R-free	0.24600 *
Structure solution method	SAD, MR
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.580
High resolution limit [Å]	1.500	1.500
Rmerge	0.064 *	0.143 *
Total number of observations	181271 *
Number of reflections	52518 *	7588 *
<I/σ(I)>	6.9
Completeness [%]	94.4	93.3
Redundancy	3.5 *	2.2 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4 *	20 *	PEG 4000, magnesium chloride, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6.0-7.8 (mg/ml)
2	1	drop		145 (mM)
3	1	drop		1 (mM)
4	1	drop	TEA-HCl	50 (mM)	pH7.4
5	1	reservoir	PEG400	30 (%(v/v))
6	1	reservoir		0.2 (M)
7	1	reservoir	HEPES	0.1 (M)	pH7.5