7LBO

Crystal structure of human Survivin bound to histone H3 T3phK4me1 peptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2013-06-20
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	C 1 2 1
Unit cell lengths	114.182, 71.441, 82.786
Unit cell angles	90.00, 129.11, 90.00

Refinement procedure

Resolution	34.340 - 2.500
R-factor	0.2097
Rwork	0.207
R-free	0.26060
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3uec
RMSD bond length	0.011
RMSD bond angle	1.457
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	2.540
High resolution limit [Å]	2.500	6.780	2.500
Rmerge	0.043	0.028	0.329
Rmeas	0.051	0.033	0.382
Rpim	0.026	0.017	0.193
Total number of observations	67635
Number of reflections	17812	879	897
<I/σ(I)>	14.8
Completeness [%]	99.5	94.3	100
Redundancy	3.8	3.5	3.8
CC(1/2)		0.998	0.954

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		289	1 uL of protein at 10 mg/mL was mixed with 1 uL of buffer composed of 0.16 M potassium/sodium tartrate, 12% PEG 3350