1NNY

Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 23 Using a Linked-Fragment Strategy

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	CCD
Collection date	2001-03-05
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 31 2 1
Unit cell lengths	89.110, 89.110, 106.210
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.850 - 2.400
R-factor	0.218
Rwork	0.195
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1TYR and initial refinement
RMSD bond length	0.009
RMSD bond angle	21.900 *
Data scaling software	HKL-2000
Phasing software	CNX (2000)
Refinement software	CNX (2000)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.075	0.420
Number of reflections	20156
<I/σ(I)>	17.75	1.4
Completeness [%]	91.0	70.6
Redundancy	4.4	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.1	277	Precipiation buffer: 100mM Hepes, 0.2 M Magnesium Acetate, 14% PEG8000, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	3-4 (mg/ml)
2	1	1	dithiothreitol	2-4 (mM)