3BI7

Crystal structure of the SRA domain of E3 ubiquitin-protein ligase UHRF1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2007-10-20
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97943
Spacegroup name	P 31 2 1
Unit cell lengths	65.975, 65.975, 96.061
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	32.990 - 1.700
R-factor	0.16043
Rwork	0.159
R-free	0.19658
Structure solution method	SAD
RMSD bond length	0.018
RMSD bond angle	1.519
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]	50.000	1.760
High resolution limit [Å]	1.700	1.700
Number of reflections	27377
<I/σ(I)>	24.15	2.1
Completeness [%]	100.0	100
Redundancy	9.9	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	298	1:1 ratio of protein (34 mg/ml) solution and well solution consisting of 1.4 M Ammonium sulfate, 0.1 M Bis-Tris pH 6.0, 0.2 M NaCl, 1 mM TCEP. Crystals cryoprotected by immersion in the well solution mixed in 1:1 ratio with a water solution containing 20% (w/v) Sucrose, 4% (w/v) Glucose, 18% (v/v) Glycerol and 18% (v/v) Ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 298K