6GE3

X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface

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	2012-03-16
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.99984
Spacegroup name	P 41 21 2
Unit cell lengths	59.149, 59.149, 158.999
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.960 - 1.850
R-factor	0.2193
Rwork	0.218
R-free	0.24210
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.066
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.960	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.068	0.704
Rmeas	0.070	0.733
Rpim	0.072	0.462
Total number of observations	321014
Number of reflections	25036
<I/σ(I)>	26.3	3.6
Completeness [%]	99.8	100
Redundancy	12.8	12.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	298	16% PEG 3350,2% tacsimate, 0.1M NaCit, pH 5.6