5QU5

Domain Swap in the first SH3 domain of human Nck1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X10SA
Synchrotron site	SLS
Beamline	X10SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-04-10
Detector	PSI PILATUS 6M
Wavelength(s)	0.99994
Spacegroup name	P 21 21 21
Unit cell lengths	40.200, 55.170, 55.230
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.030 - 1.110
R-factor	0.1551
Rwork	0.152
R-free	0.20790
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	inhouse model
RMSD bond length	0.022
RMSD bond angle	2.037
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.8.0189)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.030	39.030	1.130
High resolution limit [Å]	1.100	4.920	1.100
Rmerge	0.077	0.029	13.661
Rmeas	0.083	0.031	14.734
Total number of observations	351842
Number of reflections	48767	643	3396
<I/σ(I)>	8.16	41.65	0.1
Completeness [%]	96.4	99.2	92.2
Redundancy	7.215	6.782	7.101
CC(1/2)	0.999	1.000

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	293	5-20 mg/mL protein in 25mM HEPES\/NaOH pH7.8, 150mM NaCl mixed 60-70% with 40-30% reservoir consisting of 0.1M Bis-Tris/HCl pH5.5, 2M NaCl, 25% PEG3350