Expression and crystallization of DsbA fromStaphylococcus aureus Academic Article uri icon

abstract

  • Bacterial Dsb proteins catalyse the in vivo formation of disulfide bonds, a critical step in the stability and activity of many proteins. Most studies on Dsb proteins have focused on Gram-negative bacteria and thus the process of oxidative folding in Gram-positive bacteria is poorly understood. To help elucidate this process in Gram-positive bacteria, DsbA from Staphylococcus aureus (SaDsbA) has been focused on. Here, the expression, purification, crystallization and preliminary diffraction analysis of SaDsbA are reported. SaDsbA crystals diffract to a resolution limit of 2.1 A and belong to the hexagonal space group P6(5) or P6(1), with unit-cell parameters a = b = 72.1, c = 92.1 A and one molecule in the asymmetric unit (64% solvent content).

authors

  • Heras, B
  • Kurz, M
  • Jarrott, R
  • Byriel, KA
  • Jones, A
  • Thöny-Meyer, L
  • Martin, JL

publication date

  • November 1, 2007