1YFO

RECEPTOR PROTEIN TYROSINE PHOSPHATASE ALPHA, DOMAIN 1 FROM MOUSE

Experimental procedure

Source type	ROTATING ANODE
Source details	MACSCIENCE M18X
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1995-07-14
Detector	MACSCIENCE
Spacegroup name	P 1 21 1
Unit cell lengths	42.190, 119.840, 61.180
Unit cell angles	90.00, 110.08, 90.00

Refinement procedure

Resolution	20.000 - 2.250
R-factor	0.184
Rwork	0.184
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2hnp
RMSD bond length	0.007
RMSD bond angle	24.160 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.000	2.350
High resolution limit [Å]	2.250	2.250
Rmerge	0.046 *	0.104 *
Number of reflections	22317
<I/σ(I)>	22	7
Completeness [%]	82.4	17.4
Redundancy	2.6	1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5		PROTEIN WAS CRYSTALLIZED FROM 12% PEG 8000 0.3 M AMMONIUM ACETATE, 50 MM SODIUM ACETATE PH 5, 2 MM DTT. ETHYLENE GLYCOL 20% WAS USED AS A CRYOPROTECTANT., pH 5.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15-20 (mg/ml)
2	1	reservoir	sodium acetate	50 (mM)
3	1	reservoir	ammonium acetate	0.3 (M)
4	1	reservoir	PEG8000	12 (%(w/v))