3SO5

Crystal structure of an Immunoglobulin I-set domain of Lrig3 protein (Lrig3) from MUS MUSCULUS at 1.70 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	100
Detector technology	CCD
Collection date	2011-04-21
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.91837,0.9792,0.97892
Spacegroup name	P 43 21 2
Unit cell lengths	63.634, 63.634, 113.405
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.351 - 1.700
R-factor	0.2063
Rwork	0.206
R-free	0.21620
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	1.180
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.15)
Phasing software	SHELX
Refinement software	BUSTER-TNT (2.8.0)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	28.351	28.351	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge		0.036	0.636
Total number of observations		2046	13539
Number of reflections	26440
<I/σ(I)>	15.8	17.2	1.2
Completeness [%]	100.0	97.9	100
Redundancy	7.1	5.7	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	293	2.5M sodium chloride, 0.2M lithium sulfate, 0.1M sodium acetate pH 4.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K