3EO2

Crystal structure of the RhoGEF domain of human neuroepithelial cell-transforming gene 1 protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2008-08-11
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97945
Spacegroup name	P 64
Unit cell lengths	95.629, 95.629, 62.887
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.600
R-factor	0.215
Rwork	0.213
R-free	0.25000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2z0q
RMSD bond length	0.014
RMSD bond angle	1.123
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0044)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.690
High resolution limit [Å]	2.600	5.600	2.600
Rmerge	0.095	0.047	0.526
Number of reflections	9673
<I/σ(I)>	12.9
Completeness [%]	95.1	98.4	65.3
Redundancy	8.8	9.6	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.8		1.0M sodium citrate, 0.1M sodium cacodylate, 5% ethylene glycol, crystallized in the presence of 1:100 (w/w) subtilisin, pH 4.8, vapor diffusion, hanging drop