2NLK

Crystal structure of D1 and D2 catalytic domains of human Protein Tyrosine Phosphatase Gamma (D1+D2 PTPRG)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2006-09-19
Detector	RIGAKU RAXIS
Spacegroup name	P 21 21 2
Unit cell lengths	118.510, 133.996, 59.084
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.936 - 2.400
R-factor	0.239
Rwork	0.237
R-free	0.27400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB ENTRies 2H4V 2c7s 1rpm 1yf0 1h02 1gwz
RMSD bond length	0.015
RMSD bond angle	1.565
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.936	39.940	2.530
High resolution limit [Å]	2.400	7.590	2.400
Rmerge	0.099	0.036	0.485
Total number of observations		5889	19072
Number of reflections	37418
<I/σ(I)>	5.9	16.2	1.5
Completeness [%]	99.5	97.9	98.6
Redundancy	4.2	4.6	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	277	10% PEG 10K, 100mM Imidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
1	VAPOR DIFFUSION, SITTING DROP	8	277	10% PEG 10K, 100mM Imidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K