The chaperonin of the hyperthermophilic archaeon Sulfolobus solfataricus, briefly Ssocpn, was purified by a fast and high-yield procedure. Ssocpn, a 920 kDa-complex of two different subunits, displays a potassium-dependent ATPase activity with a temperature optimum at 80 degrees C. The ability of Ssocpn to function in vitro was investigated using different protein substrates. Ssocpn promotes correct refolding of thermophilic and mesophilic enzymes from their chemically unfolded state; moreover, Ssocpn prevents the irreversible inactivation of native proteins by suppressing their precipitation upon heating. Both the activity in assisting refolding of unfolded proteins and that in preventing heat denaturation of native proteins require the hydrolysis of ATP. The chaperone-based strategies in different technological fields are discussed, and the advantages in using archaeal chaperonins are underlined.