Purification, crystallization and preliminary X-ray diffraction analysis of the Staphylococcus epidermidis extracellular serine protease Esp

Academic Article

Abstract

  • Esp, an extracellular serine protease from Staphylococcus epidermidis, has been shown to inhibit S. aureus biofilm formation and nasal colonization. The full-length 27 kDa pro-Esp was purified and digested with thermolysin to obtain mature Esp. The mature Esp containing 216 residues crystallized in space group P21, with unit-cell parameters a = 39.5, b = 61.2, c = 42.5 Å, β = 98.2° and one molecule in the asymmetric unit, with an estimated solvent content of 42%. A diffraction data set has been collected to 1.8 Å resolution on a rotating-anode home-source facility. © 2013 International Union of Crystallography. All rights reserved.
  • Digital Object Identifier (doi)

    Author List

  • Vengadesan K; MacOn K; Sugumoto S; Mizunoe Y; Iwase T; Narayana SVL
  • Start Page

  • 49
  • End Page

  • 52
  • Volume

  • 69
  • Issue

  • 1