4WOT

ROCK2 IN COMPLEX WITH 1426382-07-1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2012-03-23
Detector	PSI PILATUS 6M
Wavelength(s)	1.00
Spacegroup name	C 1 2 1
Unit cell lengths	148.192, 148.226, 117.382
Unit cell angles	90.00, 118.65, 90.00

Refinement procedure

Resolution	103.010 - 2.930
R-factor	0.22349
Rwork	0.223
R-free	0.26806
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.143
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	103.010	3.180
High resolution limit [Å]	2.930	2.930
Rmerge	0.052	0.441
Number of reflections	47805
Completeness [%]	99.6	99.7
Redundancy	4.3	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	The purified protein was used in crystallisation trials employing both, a standard screen with approximately 1200 different conditions, as well as crystallisation conditions identified using literature data. Conditions initially obtained have been optimised using standard strategies, systematically varying parameters critically influencing crystallisation, such as temperature, protein concentration, drop ratio, and others. These conditions were also refined by systematically varying pH or precipitant concentrations. The final selected condition included PEG, at pH 6.5. Crystals were rhombic in shape and grew over a period of one week to the final size