Expression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):884-7. doi: 10.1107/S1744309113017132. Epub 2013 Jul 27.

Abstract

The spermidine acetyltransferase (SAT) from Escherichia coli catalyses the transfer of acetyl groups from acetyl-CoA to spermidine. SAT has been expressed and purified from E. coli. SAT was crystallized by the sitting-drop vapour-diffusion method to obtain a more detailed insight into the molecular mechanism. Preliminary X-ray diffraction studies revealed that the crystals diffracted to 2.5 Å resolution and belonged to the cubic space group P23, with unit-cell parameters a = b = c = 148.7 Å. They contained four molecules per asymmetric unit.

Keywords: Escherichia coli; spermidine acetyltransferase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / biosynthesis*
  • Acetyltransferases / chemistry
  • Acetyltransferases / isolation & purification*
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / biosynthesis*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / isolation & purification*
  • Gene Expression Regulation, Bacterial*

Substances

  • Escherichia coli Proteins
  • Acetyltransferases
  • diamine N-acetyltransferase