Expression, purification, crystallization and preliminary crystallographic study of FtsA from methicillin-resistant Staphylococcus aureus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):895-8. doi: 10.1107/S1744309113017727. Epub 2013 Jul 27.

Abstract

FtsA from methicillin-resistant Staphylococcus aureus (MRSA) was cloned, overexpressed and purified. The protein was crystallized using the sitting-drop vapour-diffusion technique. A cocrystal with β-γ-imidoadenosine 5'-phosphate (AMPPNP; a nonhydrolysable ATP analogue) was grown using PEG 3350 as a precipitant at 293 K. X-ray diffraction data were collected to a resolution of 2.3 Å at 100 K. The crystal belonged to the monoclinic space group P2₁, with unit-cell parameters a = 75.31, b = 102.78, c = 105.90 Å, β = 96.54°. The calculated Matthews coefficient suggested that the asymmetric unit contained three or four monomers.

Keywords: FtsA; bacterial divisome; methicillin-resistant Staphylococcus aureus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / isolation & purification*
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression Regulation, Bacterial*
  • Methicillin-Resistant Staphylococcus aureus*
  • Molecular Sequence Data

Substances

  • Bacterial Proteins
  • FtsA protein, Bacteria