Electron microscopy of biotinylated protein complexes bound to streptavidin monolayer crystals

J Struct Biol. 2012 Oct;180(1):249-53. doi: 10.1016/j.jsb.2012.04.025. Epub 2012 May 11.


Chemical biotinylation of protein complexes followed by binding to two-dimensional (monolayer) crystals of streptavidin is shown to be an effective way to prepare cryo-EM specimens from samples at low protein concentration. Three different multiprotein complexes are used to demonstrate the generality of this method. In addition, native thermosomes, purified from Sulfolobus solfataricus P2, are used to demonstrate that a uniform distribution of Euler angles is produced, even though this particle is known to adopt a preferred orientation when other methods of cryo-EM specimen preparation are used.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adsorption
  • Animals
  • Apoferritins / chemistry
  • Apoferritins / ultrastructure
  • Bacterial Proteins / chemistry
  • Biotin / chemistry*
  • Biotinylation
  • Cryoelectron Microscopy / methods*
  • Crystallization
  • Desulfovibrio vulgaris
  • Horses
  • Models, Molecular
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / ultrastructure
  • Protein Binding
  • Protein Structure, Quaternary
  • Streptavidin / chemistry*
  • Sulfolobus solfataricus
  • Thermosomes / chemistry
  • Thermosomes / ultrastructure


  • Bacterial Proteins
  • Multienzyme Complexes
  • Biotin
  • 6,7-dimethyl-8-ribityllumazine synthase
  • Streptavidin
  • Apoferritins
  • Thermosomes