Crystallization and preliminary X-ray diffraction analysis of rat protein tyrosine phosphatase eta.
The rat protein tyrosine phosphatase eta (rPTPeta) is a cysteine-dependent phosphatase which hydrolyzes phosphoester bonds in proteins and other molecules. rPTPeta and its human homologue DEP-1 are involved in neoplastic transformations. Thus, expression of the protein is reduced in all oncogene-transformed thyroid cell lines and is absent in highly malignant thyroid cells. Moreover, consistent with the suggested tumour suppression role of PTPeta, inhibition of the tumorigenic process occurs after its exogenous reconstitution, suggesting that PTPeta might be important for gene therapy of cancers. In this study, the catalytic domain of rPTPeta was produced in Escherichia coli in soluble form and purified to homogeneity. Crystals were obtained by the hanging-drop vapour-diffusion method. Diffraction data were collected to 1.87 A resolution. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.46, b = 63.07, c = 111.64 A, and contains one molecule per asymmetric unit.
Matozo
Huita C
HC
Instituto de Física de São Carlos, Departamento de Física e Informática, Universidade de São Paulo, Avenida Trabalhador São Carlense 400, CEP 13566-590 São Carlos, SP, Brazil.
Nascimento
Alessandro S
AS
Santos
Maria A M
MA
Iuliano
Rodolfo
R
Fusco
Alfredo
A
Polikarpov
Igor
I
D000818:Animals; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D021122:Protein Subunits / Q000737:chemistry* / Q000302:isolation & purification; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000302:isolation & purification; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D021122:Protein Subunits; D011994:Recombinant Proteins; D017027:Protein Tyrosine Phosphatases; C453859:phosphotyrosine phosphatase eta