5OB1

Crystal structure of the c-Src-SH3 domain Q128R 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	C 1 2 1
Unit cell lengths	65.800, 32.840, 31.580
Unit cell angles	90.00, 104.39, 90.00

Refinement procedure

Resolution	22.433 - 1.172
R-factor	0.1202
Rwork	0.119
R-free	0.14130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jz4
RMSD bond length	0.009
RMSD bond angle	1.187
Data reduction software	XDS
Data scaling software	Aimless (0.3.6)
Phasing software	PHASER
Refinement software	PHENIX ((1.11.1_2575: ???))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	22.433	22.433	1.190
High resolution limit [Å]	1.170	6.420	1.170
Rmerge	0.048	0.042	0.096
Rmeas	0.058	0.052	0.119
Rpim	0.033	0.032	0.069
Number of reflections	42089
<I/σ(I)>	17.7
Completeness [%]	97.9	64.1	87.1
Redundancy	2.9	2.3	2.5
CC(1/2)	0.995	0.991	0.981

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4	298	1.6 M Ammonium sulphate, 0.1 M sodium chloride, 0.1 M sodium acetate and 10% Glycerol