5FEA

Domain Swapped Bromodomain from Leishmania donovani

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2015-07-10
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97921
Spacegroup name	P 64 2 2
Unit cell lengths	77.176, 77.176, 169.496
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.600
R-factor	0.23
Rwork	0.228
R-free	0.27720
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5c8g
RMSD bond length	0.008
RMSD bond angle	1.136
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0124)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.640
High resolution limit [Å]	2.600	7.050	2.600
Rmerge	0.099	0.052	0.698
Rmeas	0.102	0.054	0.718
Rpim	0.025	0.014	0.165
Total number of observations	173005
Number of reflections	9764
<I/σ(I)>	10.1
Completeness [%]	98.9	96.8	98.5
Redundancy	17.7	15	18.7
CC(1/2)		0.998	0.984

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	The protein (concentrated to 15mg/mL in 20mM HEPES pH 7.5 and 150 mM NaCl) was crystallized at 293 K in 30% PEG2000 MME, 0.15M KBr with bromosporine using the sitting drop method.