3GF9

Crystal structure of human Intersectin 2 RhoGEF domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2009-02-15
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97937
Spacegroup name	C 1 2 1
Unit cell lengths	106.249, 29.616, 86.150
Unit cell angles	90.00, 121.06, 90.00

Refinement procedure

Resolution	36.899 - 2.500
R-factor	0.224
Rwork	0.221
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ki1
RMSD bond length	0.008
RMSD bond angle	1.137
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.590
High resolution limit [Å]	2.500	5.380	2.500
Rmerge	0.091	0.035	0.621
Number of reflections	8098
<I/σ(I)>	10.2
Completeness [%]	97.3	99.7	87.7
Redundancy	3.1	3.2	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291	25% PEG-3350, 0.1M ammonium sulfate, 0.1M Bis-Tris, 1:100 papain protease was added, SDS-PAGE indicated that the crystallized protein had a molecular weight of 23kDa, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K