1JB3

The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Wavelength(s)	0.95, 0.97842, 0.97928, 1.2
Spacegroup name	C 1 2 1
Unit cell lengths	76.130, 49.460, 53.280
Unit cell angles	90.00, 116.40, 90.00

Refinement procedure

Resolution	8.000 - 1.600
R-factor	0.198
Rwork	0.198
R-free	0.24300
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	1.400
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SHARP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.060 *	0.325 *
Number of reflections	22609
<I/σ(I)>	5	5
Completeness [%]	94.3	93.6 *
Redundancy	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.2 *	4 *	PEG4000, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	4 (mg/ml)
2	1	reservoir	citrate	0.1 (M)
3	1	reservoir	PEG4000	20 (%(w/v))
4	1	reservoir	2-propanol	20 (%(w/v))
5	1	reservoir	MPD	20 (%(w/v))