1LR9

STRUCTURE OF Fs1, THE HEPARIN-BINDING DOMAIN OF FOLLISTATIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2001-02-11
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9795
Spacegroup name	P 21 21 21
Unit cell lengths	21.551, 43.733, 77.376
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.600 * - 2.500
R-factor	0.22151
Rwork	0.220
R-free	0.25800 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1lr7
RMSD bond length	0.019
RMSD bond angle	1.650 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.600	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.100	0.170 *
Number of reflections	2787
Completeness [%]	98.2	90.4
Redundancy	7.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	18 *	30-35% PEG4000, 0.4 M Magnesium chloride, 0.1 M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	PEG4000	30-35 (%)
3	1	reservoir		0.4 (M)
4	1	reservoir	Tris-HCl	0.1 (M)	pH8.5