Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):228-30. doi: 10.1107/S1744309106003654. Epub 2006 Feb 10.

Abstract

Sso6206, a 10.5 kDa protein from Sulfolobus solfataricus, has been overexpressed, purified and crystallized. The protein crystallizes in space group P6(1/5)22, with unit-cell parameters a = b = 157.8, c = 307.3 A. The crystals are hexagonal bipyramids and a data set has been collected to 2.4 A resolution. Molecular replacement cannot be attempted as no convincing model can be identified. Crystals of selenomethionine-variant protein have not yet been obtained. Interestingly, crystal packing, gel filtration and mass spectrometry all suggest the native protein forms a multi-subunit oligomer consisting of >9 subunits.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Archaeal Proteins / biosynthesis
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / isolation & purification
  • Cloning, Molecular
  • Crystallization / methods
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Molecular Sequence Data
  • Protein Structure, Quaternary
  • Sequence Alignment
  • Sulfolobus solfataricus / chemistry*

Substances

  • Archaeal Proteins