FORMATION INVIVO, PURIFICATION AND CRYSTALLIZATION OF A COMPLEX OF THE GAMMA-SUBUNIT AND EPSILON-SUBUNIT OF THE F0F1-ATPASE OF ESCHERICHIA-COLI

A complex comprising the ε subunit of Escherichia coli F1-ATPase (ECF1-ATPase) and a glutathione-S-transferase γ subunit (of ECF1-ATPase) fusion protein was formed in vivo and purified from cell extracts by binding to glutathione-agarose beads. The glutathione-S-transferase was released from the complex by digestion with thrombin and the γ/ε complex purified by cation-exchange chromatography. Crystals of the complex were grown by vapour diffusion using PEG8000 as precipitant. The crystals are orthorhombic, space-group P21212 with a = 161.9 Å, b = 44.1 Å and c = 63.4 Å. The volume of the asymmetric unit is consistent with the presence of a complex of one γ subunit and one ε subunit. © 1993 Academic Press, Inc.