1KAK

Human Tyrosine Phosphatase 1B Complexed with an Inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	100
Detector technology	CCD
Collection date	1998-08-16
Detector	ADSC QUANTUM 4
Wavelength(s)	0.948
Spacegroup name	P 31 2 1
Unit cell lengths	87.516, 87.516, 106.287
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.500
R-factor	0.189
Rwork	0.189
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Native PTP1B structure (2HNP)
RMSD bond length	0.008 *
RMSD bond angle	1.470 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.560
High resolution limit [Å]	2.500	2.500
Rmerge	0.054 *
Total number of observations	61055 *
Number of reflections	13400 *
<I/σ(I)>	14.8	8.1
Completeness [%]	80.0 *	96.5
Redundancy	1.4	23

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5 *	4 *	Barford, D., (1994) J. Mol. Biol., 239, 726. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PTP1B	10 (mg/ml)
2	1	reservoir	HEPES	0.1 (M)	pH7.5
3	1	reservoir	magnesium acetate	0.2 (M)
4	1	reservoir	PEG8000	12-16 (%(w/v))