Crystallization and preliminary X-ray analysis of Drosophila glutathione S-transferase-2

Abstract

The σ-class glutathione S-transferase-2 (GST-2) from Drosophila melanogaster is predominantly found within the indirect flight muscles (IFMs), where it is bound to the `heavy' subunit of the IFM thin filament troponin complex (Tn-H). An N-terminal extension found in GST-2 is unique within the σ GST class and may be involved in its interaction with Tn-H or modulate its enzymatic function. The recombinant protein has been crystallized at room temperature using ammonium sulfate as precipitant. Synchrotron radiation was used to measure a complete native data set to 1.75 Å resolution from flash-cooled crystals. The crystals belong to one of the trigonal space groups P3121 or P3221, with unit-cell parameters a = b = 89.7, c = 131.8 Å. The self-rotation function is consistent with a GST-2 dimer in the asymmetric unit.