Crystallization and preliminary crystallographic analysis of nosiheptide-resistance methyltransferase from Streptomyces actuosus in complex with SAM

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt 5):579-82. doi: 10.1107/S1744309110011395. Epub 2010 Apr 30.


Nosiheptide-resistance methyltransferase (NSR) methylates 23S rRNA at the nucleotide adenosine 1067 in Escherichia coli and thus contributes to resistance against nosiheptide, a sulfur-containing peptide antibiotic. Here, the expression, purification and crystallization of NSR from Streptomyces actuosus are reported. Diffracting crystals were grown by the hanging-drop vapour-diffusion method in reservoir solution consisting of 0.35 M ammonium chloride, 24%(w/v) PEG 3350, 0.1 M MES pH 5.7 at 293 K. Native data have been collected from the apo enzyme and a SAM complex, as well as apo SeMet SAD data. The diffraction patterns of the apo form of NSR, of NSR complexed with SAM and of SeMet-labelled NSR crystals extended to 1.90, 1.95 and 2.25 A resolution, respectively, using synchrotron radiation. All crystals belonged to space group P2(1), with approximate unit-cell parameters a = 64.6, b = 69.6, c = 64.9 A, beta = 117.8 degrees .

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Drug Resistance, Bacterial*
  • Methyltransferases / chemistry*
  • Methyltransferases / metabolism
  • S-Adenosylmethionine / chemistry*
  • S-Adenosylmethionine / metabolism
  • Streptomyces / drug effects
  • Streptomyces / enzymology*
  • Thiazoles / pharmacology


  • Thiazoles
  • S-Adenosylmethionine
  • Methyltransferases
  • nosiheptide