Purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytoplasmic domain of FlhB from Salmonella typhimurium

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):808-11. doi: 10.1107/S1744309111018938. Epub 2011 Jun 30.

Abstract

FlhB is a key protein in the regulation of protein export by the bacterial flagellar secretion system. It is composed of two domains: an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhBc). FlhBc from Salmonella typhimurium has been successfully crystallized using the vapour-diffusion method. The crystals diffracted to 2.45 Å resolution and belonged to space group P4(2)2(1)2, with unit-cell parameters a=b=49.06, c=142.94 Å. A selenomethionine-containing variant of FlhBc has also been crystallized in the same space group and was used for initial phase calculation by the multiwavelength anomalous dispersion (MAD) method.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Cytoplasm / chemistry
  • Membrane Proteins / chemistry*
  • Membrane Proteins / isolation & purification
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Salmonella typhimurium / chemistry*
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • FlhB protein, Bacteria
  • Membrane Proteins