7LBQ

Crystal structure of human Survivin bound to histone H3 T3phK4me2 peptide

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	2012-11-08
Detector	ADSC QUANTUM 210
Wavelength(s)	0.97926
Spacegroup name	I 2 2 2
Unit cell lengths	69.343, 70.162, 89.447
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.360 - 2.690
R-factor	0.2494
Rwork	0.248
R-free	0.26840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3uec
RMSD bond length	0.017
RMSD bond angle	2.063
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.7.0029)

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	0.075	0.059	0.758
Total number of observations	43026
Number of reflections	6766	325	356
<I/σ(I)>	18.2
Completeness [%]	99.1	84.4	100
Redundancy	6.4	5.1	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	289	1 uL of protein was mixed with 1uL of buffer composed of 2.25 mM spermine, 9 mM MgCl2, 0.9 mM spermidine, 1.8 mM cobalt (III)hexamine chloride, 0.05 sodium cacodylate pH 7.0, 5% PEG 400