5KO4

Bromodomain from Trypanosoma brucei Tb427.10.8150

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2016-04-03
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97901
Spacegroup name	P 1 21 1
Unit cell lengths	45.374, 52.756, 47.027
Unit cell angles	90.00, 117.27, 90.00

Refinement procedure

Resolution	41.800 - 1.440
R-factor	0.162
Rwork	0.161
R-free	0.17600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3o33
RMSD bond length	0.008
RMSD bond angle	0.740
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	BALBES
Refinement software	BUSTER (2.10.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.460
High resolution limit [Å]	1.440	1.440
Rmerge	0.082	0.358
Number of reflections	35635
<I/σ(I)>	9.1
Completeness [%]	99.2	96.5
Redundancy	6.7	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	The 12 mg/ml (0.95 mM) protein in the base buffer (100 mM NaCl, 0.5 mM TCEP, 20 mM HEPES pH7,5) was crystallized at 20 ??C in 30% PEGM5K, 0.2 M NH4SO4, 0.1 M MES pH 6.5, in vapor diffusion sitting drop method. Final concentration of 3% DMSO and 1 mM SGC-CBP30 (IUPAC name: 8-(3-chloro-4-methoxy-phenethyl)-4-(3,5-dimethyl-isoxazol-4-yl)-9-(2-(morpholin-4-yl)-propyl)-7,9-diaza-bicyclo[4.3.0]nona-1(6),2,4,7-tetraene) was added to the concentrated protein immediately prior to setting up the crystallization plate.