2EFK

Crystal structure of the EFC domain of Cdc42-interacting protein 4

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2005-08-19
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9794, 0.9795, 1.0000
Spacegroup name	C 1 2 1
Unit cell lengths	94.817, 70.410, 65.679
Unit cell angles	90.00, 107.20, 90.00

Refinement procedure

Resolution	45.290 - 2.300
R-factor	0.228
Rwork	0.228
R-free	0.27900
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	1.000
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.072	0.317
Number of reflections	16924
<I/σ(I)>	21.1	3.5
Completeness [%]	91.7	61.2
Redundancy	4.9	4.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	SMALL TUBES	8	277	20mM Tris-HCl, 150mM NaCl, 2mM DTT, pH 8.0, SMALL TUBES, temperature 277K
1	SMALL TUBES	8	277	20mM Tris-HCl, 150mM NaCl, 2mM DTT, pH 8.0, SMALL TUBES, temperature 277K
1	SMALL TUBES	8	277	20mM Tris-HCl, 150mM NaCl, 2mM DTT, pH 8.0, SMALL TUBES, temperature 277K