5OB0

Crystal structure of the c-Src-SH3 domain Q128E mutant in complex with the high affinity peptide APP12

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2013-02-24
Detector	MARRESEARCH
Wavelength(s)	0.9334
Spacegroup name	I 1 2 1
Unit cell lengths	31.630, 32.560, 65.262
Unit cell angles	90.00, 103.02, 90.00

Refinement procedure

Resolution	25.000 - 1.172
R-factor	0.132
Rwork	0.131
R-free	0.14910
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ZJ4
RMSD bond length	0.009
RMSD bond angle	1.164
Data reduction software	XDS
Data scaling software	Aimless (0.3.11)
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	25.000	25.560	1.190
High resolution limit [Å]	1.170	6.420	1.170
Rmerge	0.074	0.046	0.166
Rmeas	0.091	0.056	0.210
Rpim	0.053	0.032	0.127
Number of reflections	41471
<I/σ(I)>	6.9
Completeness [%]	97.3	56.4	94.6
Redundancy	2.6	2.4	2.1
CC(1/2)	0.993	0.989	0.936

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4	298	1.9 M Ammonium sulphate, 0.05 M sodium chloride, 0.1 M sodium acetate and 10% Glycerol