3LMN

Oligomeric structure of the DUSP domain of human USP15

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E SUPERBRIGHT
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2010-01-07
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.54178
Spacegroup name	I 41 2 2
Unit cell lengths	138.174, 138.174, 132.114
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.520 - 2.150
R-factor	0.18442
Rwork	0.183
R-free	0.20401
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3jyu
RMSD bond length	0.012
RMSD bond angle	1.209
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.190
High resolution limit [Å]	2.150	2.150
Number of reflections	35029
<I/σ(I)>	35.89	3.62
Completeness [%]	100.0	100
Redundancy	14.3	14.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3.8	291.1	Crystals of the dusp domain of usp15 were grown at 291.1 K using the sitting drop method by mixing equal volumes of protein solution (15 mg/ml) and crystallization buffer (2.0 M ammonium formate, 0.1 M sodium acetate, pH 3.8.) The crystals were cryoprotected by immersion in well solution supplemented with 20% (v/v) glycerol prior to dunking and storage in liquid nitrogen., VAPOR DIFFUSION, SITTING DROP