6AFR

Crystal Structure of the first bromodomain of human BRD4 in complex with 5-((4-fluoro-1H-imidazol-1-yl)methyl)quinolin-8-ol

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL17U
Synchrotron site	SSRF
Beamline	BL17U
Temperature [K]	80
Detector technology	CCD
Collection date	2018-07-04
Detector	Nonius Kappa CCD
Wavelength(s)	0.9
Spacegroup name	P 21 21 21
Unit cell lengths	31.980, 47.208, 78.737
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.370 - 1.998
R-factor	0.2145
Rwork	0.212
R-free	0.26770
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.911
Refinement software	PHENIX ((1.12_2829: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	39.370	2.069
High resolution limit [Å]	1.998	1.998
Number of reflections	8538
<I/σ(I)>	12.44
Completeness [%]	99.8
Redundancy	12.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4	289.15	The protein was concentrated to 8-10 mg mL-1 in the buffer containing 20mM HEPES, pH7.4, 100mM NaCl and 1mM DTT. The apo crystals of BRD4_BD1 were harvested by using sitting drop vapor-diffusion method in 4M sodium formate and 15% glycerol at 289.15K. Then the apo crystals were soaked into reservoir solution containing 1mM compound for 7 days.