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

The sigma -class glutathione S-transferase-2 (GST-2) from Drosophila melano gaster is predominantly found within the indirect flight muscles (IFMs), wh ere it is bound to the 'heavy' subunit of the IFM thin filament troponin co mplex (Tn-H). An N-terminal extension found in GST-2 is unique within the s igma GST class and may be involved in its interaction with Tn-H or modulate its enzymatic function. The recombinant protein has been crystallized at r oom temperature using ammonium sulfate as precipitant. Synchrotron radiatio n was used to measure a complete native data set to 1.75 Angstrom resolutio n from flash-cooled crystals. The crystals belong to one of the trigonal sp ace groups P3(1)21 or P3(2)21, with unit-cell parameters a = b = 89.7, c = 131.8 Angstrom. The self-rotation function is consistent with a GST-2 dimer in the asymmetric unit.