Three-dimensional Reconstruction of the Surface Protein of the Extremely Thermophilic Archaebacterium Archaeoglobus fulgidus

Martin Kessel, Susanne Volker, Ute Santarius, Robert Huber, Wolfgang Baumeister*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The three-dimensional structure of the regular cell surface of Archaeoglobus fulgidus has been determined to a resolution of 1.8 nm. Envelopes prepared by freezing and thawing the cells were treated for 2 sec with 0.01% SDS to ensure optimal negative staining of the cell surface morphological units, which are arranged on an hexagonal lattice with a center to center spacing of 17.5 nm. The three-dimensional structure reveals the morphological unit to be dome-shaped with a wide opening to the cell membrane and a narrow opening to the exterior at the apex. This design principle is reminiscent of H. volcanii and, to a lesser extent of Sulfolobus solfataricus. The morphological units show little evidence of connectivity and the integrity of the lattice appears to rely on the interaction with the cell membrane.

Original languageEnglish
Pages (from-to)207-213
Number of pages7
JournalSystematic and Applied Microbiology
Volume13
Issue number3
DOIs
StatePublished - 1990

Keywords

  • Archaebacteria
  • Archaeoglobus fulgidus
  • Cell envelope
  • S-Layer
  • Three dimensional structure

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