1FPR

CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	85
Detector technology	IMAGE PLATE
Collection date	1998-08-08
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	111.580, 45.210, 56.270
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	6.000 - 2.500
R-factor	0.194 *
Rwork	0.194
R-free	0.30300
RMSD bond length	0.007
RMSD bond angle	1.400
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall
High resolution limit [Å]	2.500
Rmerge	0.097
Total number of observations	27345 *
Number of reflections	8998 *
Completeness [%]	85.0

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	8.5	277	ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	ammonium sulfate	1.9 (M)
3	1	reservoir	Tris-HCl	0.1 (M)