The enzymatic activity of SHP2, whose dysregulation causes malfunctions in diverse cellular signaling, is controlled by the autoinhibitory association between its N-SH2 and phosphatase domains. Various SHP2 genetic mutations, which impair the interaction between the two domains, have been identified to cause RAS-MAPK pathway-associated diseases. In this study, SHP2 containing Noonan syndrome-associated T2I and L262F double mutations was targeted for crystallization. The recombinant protein was prepared using an Escherichia coli expression system, purified using Ni-NTA affinity and size exclusion chromatographies, and then subjected for crystallization. X-ray data diffracted to 3.0 Å resolution were collected and used for preliminary diffraction analysis. The unit cell parameters of the crystals belonging to the P2₁ space group were a = 45.4 Å, b = 215.0 Å, c = 55.6 Å, and β = 95.7°. The asymmetric unit contains two molecules with a solvent content of 40.7% and a Matthews coefficient of 2.07 ų/Da.