2O25

Ubiquitin-Conjugating Enzyme E2-25 kDa Complexed With SUMO-1-Conjugating Enzyme UBC9

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	100
Detector technology	CCD
Collection date	2006-05-07
Detector	ADSC QUANTUM 210
Wavelength(s)	0.91841
Spacegroup name	P 1
Unit cell lengths	41.874, 68.498, 91.277
Unit cell angles	85.05, 80.85, 75.83

Refinement procedure

Resolution	30.000 - 2.600
R-factor	0.23105
Rwork	0.228
R-free	0.29091
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB entries 1YLA and 1A3S
RMSD bond length	0.016
RMSD bond angle	1.624
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.640
High resolution limit [Å]	2.600	2.600
Number of reflections	27651
<I/σ(I)>	13.9	2.17
Completeness [%]	93.3	70.8
Redundancy	1.9	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	298	The protein complex (1:1) was dissolved at 26 mg/ml in 20 mM Tris-HCl, pH 8.0, 5% glycerol, 2 mM DTT. Hanging drops (2 microL + 2 microL), room temperature, well solution: 16% PEG MME 5000, 0.1 M bis-Tris, pH 6.0, 1 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K