2ONI

Catalytic Domain of the Human NEDD4-like E3 Ligase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2006-12-09
Detector	ADSC QUANTUM 210
Wavelength(s)	0.97922
Spacegroup name	P 63 2 2
Unit cell lengths	103.058, 103.058, 182.214
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	28.280 - 2.200
R-factor	0.20896
Rwork	0.206
R-free	0.25916
Structure solution method	SAD
RMSD bond length	0.017
RMSD bond angle	1.543
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	SOLVE
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.280
High resolution limit [Å]	2.200	2.200
Number of reflections	29656
<I/σ(I)>	35.3	3.3
Completeness [%]	99.7	99.9
Redundancy	11	11.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	294	THE PROTEIN WAS DISSOLVED AT 10 mg/mL IN 10 mM TRIS-HCL, PH 8.0, 100 mM NaCl, 2% GLYCEROL AND 1 mM DTT. CRYSTALS WERE GROWN BY VAPOR DIFFUSION, HANGING DROPS BY MIXING 2 MICROL PROTEIN SOLUTION WITH 2 MICROL WELL SOLUTION (1.7 M SODIUM/POTASSIUM PHOSPHATE, PH 6.0, 1 mM DTT) AT TEMPERATURE 294.0K. FOR CRYOPROTECTION, THE CRYSTALS WERE SOAKED IN 2 M SODIUM-POTASSIUM PHOSPHATE, pH 7.0, 1 mM DTT, 25% ETHYLENE GLYCOL AND 2 mG/mL SEMETNEDD4L.574.947.