Crystallization of the cpn60/cpn10 complex ('holo-chaperonin') from Thermus thermophilus

FEBS Lett. 1992 Oct 12;311(1):22-4. doi: 10.1016/0014-5793(92)81357-r.

Abstract

A stable complex of the chaperonins, cpn60 and cpn10 (Escherichia coli GroEL and GroES homologues), from the extremely thermophilic bacterium Thermus thermophilus has been isolated and crystallized. The crystals have dimensions up to 30 x 200 x 200 microns. Ultra-thin sections of the crystals estimated by electron microscopy showed a rectangular lattice with unit cell parameters of a = 17 nm, b = 27 nm, gamma = 90 degrees.

MeSH terms

  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / ultrastructure
  • Chaperonin 10
  • Chaperonin 60
  • Chaperonins
  • Crystallization
  • Heat-Shock Proteins / isolation & purification*
  • Heat-Shock Proteins / ultrastructure
  • Macromolecular Substances
  • Proteins / isolation & purification*
  • Proteins / ultrastructure
  • Thermus thermophilus / chemistry*

Substances

  • Bacterial Proteins
  • Chaperonin 10
  • Chaperonin 60
  • Heat-Shock Proteins
  • Macromolecular Substances
  • Proteins
  • Chaperonins