Two-dimensional crystals of reconstituted beta-subunits of the chaperonin TF55 from Sulfolobus shibatae

Biochim Biophys Acta. 1998 Dec 8;1429(1):40-4. doi: 10.1016/s0167-4838(98)00218-0.

Abstract

We have obtained 2-dimensional crystals of the beta-subunits of the chaperonin TF55 from Sulfolobus shibatae reconstituted into oligomers in the absence of alpha-subunits. The subunits form rings with 9-fold rotational symmetry which arrange themselves in a trigonal lattice. From electron micrographs of negatively stained specimens we have calculated a projection map in plane group p312 showing the rings in top-view.

MeSH terms

  • Archaeal Proteins
  • Crystallization
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / isolation & purification*
  • Microscopy, Electron
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / isolation & purification*
  • Mutagenesis, Site-Directed
  • Sulfolobus / metabolism*

Substances

  • Archaeal Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • TF55 protein, Sulfolobus shibatae