The D. melanogaster σ-class GST has been expressed, purified and crystallized. The crystals diffract to at least 1.75 Å resolution using synchrotron radiation.

The preparation and successful crystallization of the Grb7 SH2 domain in complex with the specific cyclic peptide inhibitor G7-18NATE are reported. This structure is anticipated to reveal the basis of the binding affinity and specificity and to assist with the development of second-generation inhibitors of Grb7, which is involved in cancer progression.