3QLC

Complex structure of ATRX ADD domain bound to unmodified H3 1-15 peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	CCD
Collection date	2010-05-20
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9795
Spacegroup name	P 32 2 1
Unit cell lengths	80.607, 80.607, 136.173
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	38.054 - 2.500
R-factor	0.198
Rwork	0.194
R-free	0.24080
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3qln
RMSD bond length	0.009
RMSD bond angle	1.206
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	PHENIX (1.6.4_486)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.560
High resolution limit [Å]	2.500	6.160	2.500
Rmerge	0.063	0.044	0.532
Number of reflections	18318
<I/σ(I)>	14.3
Completeness [%]	99.7	96.6	100
Redundancy	12.4	12.9	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	24% PEG 3350, 0.1M HEPES-NaOH, 0.2M KCL, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K