GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution

CroES consists of seven identical 10 kDa subunits and is involved in assisting protein folding as the partner of another oligomeric protein, the GroEL chaperonin. Wore we studied the GroES structure in solution using small-angle X-ray scattering (SAXS), The SASS pattern, calculated for the CroES crystal structure, was found to be different from the experimental one measured in solution. The synchronic shift in the radial direction and some turning of the protein subunits eliminate the difference and result in the incase of the hole diameter in the GroES ring-like structure from 8 Angstrom in the crystal to 21 Angstrom in solution. (C) 2000 Federation of European Biochemical Societies.