2E3V

Crystal structure of the first fibronectin type III domain of neural cell adhesion molecule splicing isoform from human muscle culture lambda-4.4

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B2
Synchrotron site	SPring-8
Beamline	BL26B2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-10-03
Detector	RIGAKU JUPITER 210
Wavelength(s)	0.979274, 0.979740, 0.964000
Spacegroup name	P 31
Unit cell lengths	55.378, 55.378, 118.830
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 1.950
R-factor	0.183
Rwork	0.182
R-free	0.21100
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	1.275
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.980
High resolution limit [Å]	1.950	1.950
Number of reflections	29327
<I/σ(I)>	36.1	3.38
Completeness [%]	98.5	80.6
Redundancy	10	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	22-25% PEG 3350, 0.1M Bis-Tris-HCl, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	22-25% PEG 3350, 0.1M Bis-Tris-HCl, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	22-25% PEG 3350, 0.1M Bis-Tris-HCl, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K