4J1Y

The X-ray crystal structure of human complement protease C1s zymogen

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	CCD
Collection date	2011-03-29
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.953695
Spacegroup name	C 2 2 2
Unit cell lengths	149.890, 158.900, 78.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	54.273 - 2.664
R-factor	0.2034
Rwork	0.201
R-free	0.25880
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1elv
RMSD bond length	0.011
RMSD bond angle	1.524
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	BALBES (/ MOLREP)
Refinement software	PHENIX ((phenix.refine: dev_1048))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	63.810	63.810	2.730
High resolution limit [Å]	2.660	11.920	2.660
Rmerge	0.093	0.040	1.125
Number of reflections	27108
<I/σ(I)>		48.9	2.5
Completeness [%]	99.3	97	97.8
Redundancy	12.2	10.6	9.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	293	18% PEG 3350, 0.2M potassium nitrate., pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K