4DJ9

Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2009-08-06
Detector	RAYONIX MX-300
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	33.540, 68.160, 137.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	68.800 - 2.250
R-factor	0.2095
Rwork	0.208
R-free	0.24720
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.120
Data reduction software	XDS ((VERSION December 6)
Data scaling software	autoPROC
Refinement software	BUSTER (2.13.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	68.800	2.258
High resolution limit [Å]	2.250	2.251
Rmerge	0.065	0.592
Number of reflections	15637
<I/σ(I)>	16.4	3.3
Completeness [%]	99.7	100
Redundancy	7	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5		The human vinculin Vh1 domain (residues 1 - 258) was generated as described.9 Crystallization screens of Vh1 protein and VBS50 mixed in 1:5 molar ratio were performed at two temperatures. Co-crystals were obtained from Hampton crystal screen I with a reservoir of 0.1 M Hepes pH 7.5, 10% w/v polyethylene glycol 6,000, and 5% 2-Methyl-2,4-pentanediol. Crystals were transferred directly from the initial 96-well screening plate into Paratone-N oil and flash-frozen in liquid nitrogen. , VAPOR DIFFUSION