2G7I

Structure of Human Complement Factor H Carboxyl Terminal Domains 19-20: a Basis for Atypical Hemolytic Uremic Syndrome

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2003-10-14
Detector	MARRESEARCH
Wavelength(s)	0.934
Spacegroup name	I 41 2 2
Unit cell lengths	91.410, 91.410, 110.880
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.780 - 1.750
R-factor	0.20735
Rwork	0.206
R-free	0.22479
Structure solution method	SAD
RMSD bond length	0.019
RMSD bond angle	1.645
Data reduction software	XDS
Data scaling software	XDS
Phasing software	SHELXS
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	14.780	1.795
High resolution limit [Å]	1.750	1.750
Number of reflections	22700
<I/σ(I)>		3.7
Completeness [%]	99.9	99.9
Redundancy	6.9	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	298	Before crystallization the protein was concentrated to 10 mg/ml and dialysed into 20 mM Tris, 50 mM NaCl, pH 7.0. The protein was crystallized in sitting drops by mixing 1 ul of protein solution at 10 mg/ml with 1 ul of reservoir solution of 2.2 M (NH4)2SO4, 0.1 M Tris-HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K
1	VAPOR DIFFUSION, SITTING DROP	8.5	298	Before crystallization the protein was concentrated to 10 mg/ml and dialysed into 20 mM Tris, 50 mM NaCl, pH 7.0. The protein was crystallized in sitting drops by mixing 1 ul of protein solution at 10 mg/ml with 1 ul of reservoir solution of 2.2 M (NH4)2SO4, 0.1 M Tris-HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K