5C11

Crystal Structure of Jarid1a PHD finger bound to histone H3C4me3 peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL17U
Synchrotron site	SSRF
Beamline	BL17U
Temperature [K]	100
Detector technology	CCD
Collection date	2014-09-14
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9792
Spacegroup name	I 4 3 2
Unit cell lengths	108.910, 108.910, 108.910
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.462 - 2.803
R-factor	0.2483
Rwork	0.245
R-free	0.27890
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3gl6
RMSD bond length	0.003
RMSD bond angle	0.698
Data scaling software	HKL-2000
Phasing software	MOLREP (11.2.05)
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.870
High resolution limit [Å]	2.800	6.900	2.800
Rmerge	0.065	0.042	0.798
Total number of observations	50009
Number of reflections	2920
<I/σ(I)>	14.3
Completeness [%]	99.5	94.5	100
Redundancy	17.1	15.2	14.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	277	0.02 M sodium l-glutamate, 0.02 M dl-alanine, 0.02 M glycine, 0.02 M dl-lysine HCl, 0.02 M dl-serine, 0.1 M Tris, 0.1 M Bicine, PH8.5, 12.5% MPD, 12.5% PEG 1K, 12.5% PEG 3350