Crystallization of the crenarchaeal SRP core

Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):140-3. doi: 10.1107/s0907444903023734. Epub 2003 Dec 18.

Abstract

Protein translocation across or targeting to membranes mediated by the signal recognition particle (SRP) is a universal mechanism conserved in all domains of life. SRP54 from the crenarchaeon Sulfolobus solfataricus has been recombinantly expressed and crystallized with and without SRP RNA helix 8. The RNA has been transcribed in vitro using ribozyme technology. Both crystal forms are perfect merohedral twins. While SRP54 alone is hemihedrally twinned, the crystals of the SRP54-helix 8 complex indicate tetartohedral twinning, which has not previously been observed in protein crystals. The tetartohedral twinning is enabled by a special diamond-like packing in a trigonal crystal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Chromatography, Affinity
  • Chromatography, Gel
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • DNA, Archaeal / chemistry
  • DNA, Archaeal / genetics
  • Escherichia coli / genetics
  • Models, Molecular
  • Polymerase Chain Reaction
  • Protein Conformation
  • RNA, Archaeal / chemistry
  • Signal Recognition Particle / chemistry*
  • Signal Recognition Particle / genetics
  • Sulfolobus / chemistry*
  • Sulfolobus / genetics
  • Sulfolobus / metabolism

Substances

  • Archaeal Proteins
  • DNA, Archaeal
  • RNA, Archaeal
  • Signal Recognition Particle