3UIG

crystal structure of human Survivin in complex with T3 phosphorylated 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	2010-12-10
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9795
Spacegroup name	C 1 2 1
Unit cell lengths	115.778, 71.042, 82.287
Unit cell angles	90.00, 128.81, 90.00

Refinement procedure

Resolution	31.072 - 2.400
R-factor	0.2151
Rwork	0.213
R-free	0.25010
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f3h
RMSD bond length	0.010
RMSD bond angle	1.224
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX ((phenix.refine: 1.6.4_486))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.052	0.527
Number of reflections	20244
<I/σ(I)>	17.2	2
Completeness [%]	97.9	86.9
Redundancy	4.1	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	0.1 M DL-malic acid, pH 7.0, 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K