5U9N

Second Bromodomain of cdg4_1340 from Cryptosporidium parvum, complexed with bromosporine

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	2016-11-25
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97600
Spacegroup name	F 2 2 2
Unit cell lengths	62.119, 186.124, 195.176
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.540 - 2.400
R-factor	0.226
Rwork	0.225
R-free	0.25600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4py6
RMSD bond length	0.010
RMSD bond angle	0.610
Data scaling software	Aimless (0.5.29)
Phasing software	PHASER
Refinement software	BUSTER (2.10.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	33.670	33.670	2.490
High resolution limit [Å]	2.400	8.970	2.400
Rmerge	0.100	0.072	0.639
Rmeas	0.108
Rpim	0.041
Total number of observations	159515
Number of reflections	22425
<I/σ(I)>	18
Completeness [%]	99.8	96.8	98.6
Redundancy	7.1	6.2	6.9
CC(1/2)	0.996	0.995	0.800

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	The protein was crystallized at 293 K in 2.5M ammonium sulfate, 0.1 M bis-tris propane pH 7.0. Bromosporine (ethyl (3-methyl-6-{4-methyl-3-[(methylsulfonyl)amino]phenyl}[1,2,4]triazolo[4,3- b]pyridazin-8-yl)carbamate) was added (final concentration of 1 mM)directly to the concentrated protein immediately prior to setting up the crystallization plate