4HVV

Crystal structure of the T98E c-Src-SH3 domain 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	2011-04-08
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97
Spacegroup name	P 31 2 1
Unit cell lengths	31.588, 31.588, 106.689
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.097 - 1.100
R-factor	0.1442
Rwork	0.144
R-free	0.15630
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3fj5
RMSD bond length	0.009
RMSD bond angle	1.214
Data reduction software	XDS
Data scaling software	Aimless (0.1.27)
Phasing software	PHASER
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.563	19.100	1.120
High resolution limit [Å]	1.100	5.920	1.100
Rmerge	0.067	0.066	0.667
Total number of observations		1474	4855
Number of reflections	24885
<I/σ(I)>	19.9	28.9	2.4
Completeness [%]	95.4	70.1	68.5
Redundancy	9.6	9.7	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	298	1.7 M Ammonium sulphate, 10% PEG 300, 10% glycerol and 0.1 M sodium acetate, pH 5, vapor diffusion, hanging drop, temperature 298K