Crystallization and preliminary X-ray diffraction analysis of rat protein tyrosine phosphatase eta

Abstract

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.

Figure 1

Crystal of rPTPηCD. Typical dimensions are approximately 0.2 × 0.4 × 0.2 mm.

Figure 2

Diffraction pattern of the rPTPηCD crystal collected on the MX-1 beamline at LNLS. The maximum resolution at the edge of the image is 1.87 Å.