7LZQ

Crystal structure of the BCL6 BTB domain in complex with OICR-4425

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2011-05-25
Detector	APEX II CCD
Wavelength(s)	1.54
Spacegroup name	C 1 2 1
Unit cell lengths	30.412, 71.626, 54.937
Unit cell angles	90.00, 104.78, 90.00

Refinement procedure

Resolution	27.200 - 1.710
R-factor	0.1578
Rwork	0.156
R-free	0.19360
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1r28
RMSD bond length	0.015
RMSD bond angle	1.674
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.210	1.740
High resolution limit [Å]	1.710	1.710
Rmerge	0.026	0.127
Rmeas	0.030	0.153
Rpim	0.015	0.083
Number of reflections	12163	1464
<I/σ(I)>	30.7	7.6
Completeness [%]	96.8	80.5
Redundancy	3.9	3
CC(1/2)	0.999	0.989

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	Protein (Bcl6 BTB domain(1-129) 13 mg/ml in protein buffer( 20 mM Tris pH 8.3, 300 mM NaCl, 10% glycerol, 1 mM TECEP)) was mixed 1:1 with reservoir buffer (1.3M sodium formate, 0.1M Na acetate pH 5.2. Ostwald ripening of the early appearing crystals took place over about 5 days. To affect a partial dehydration the reservoir buffer was exchanged in 0.5 M steps to 4 M Na formate/0.1M Na acetate pH 5.2. In separate wells drops of soaking buffer ((1 M Na formate, 5% glycerol, 50 mM Na acetate pH5.2, 10 mM Tris pH 8.3, 150 mM NaCl) was also equilibrated against the 4 M formate/acetate. Crystals were transferred to equilibrated soaking buffer to which 2.5 mM OICR-4425 and 5% DMSO had been added.