3IDO

Crystal structure of protein tyrosine phosphatase from Entamoeba histolytica with a phosphotyrosine crude mimic HEPES molecule in the active site

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2009-07-11
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9765
Spacegroup name	P 21 21 21
Unit cell lengths	60.579, 70.409, 79.189
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.930 - 2.200
R-factor	0.206
Rwork	0.204
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1xww
RMSD bond length	0.010
RMSD bond angle	1.211
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.930	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.140	0.492
Number of reflections	17494
<I/σ(I)>	7.7	2.43
Completeness [%]	98.6	89.5
Redundancy	8.1	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	ProPlex condition F1, 0.1 M Hepes pH 7.0, 20% PEG 8000, 25% glycerol as cryo-protectant, 26.1 mg/mL protein, 0.1 mg/mL chymotrypsin, crystal tracking ID 203694f1, VAPOR DIFFUSION, SITTING DROP, temperature 289K