Crystallization and preliminary X-ray crystallographic analysis of Ace: a collagen-binding MSCRAMM from Enterococcus faecalis.

Academic Article

Abstract

  • Ace is a collagen-binding bacterial cell surface adhesin from Enterococcus faecalis. The collagen-binding domain of Ace (termed Ace40) and its truncated form Ace19 have been crystallized by the vapor-diffusion hanging-drop method. Ace19 was crystallized in two different crystal forms. A complete 1.65 A data set has been collected on the orthorhombic crystal form with unit cell parameters a=38.43 b=48.91 and c=83.73 A. Ace40 was crystallized in the trigonal space group P3(1)21 or P3(2)21 with unit cell parameters a=b=80.24, c=105.91 A; alpha=beta=90 and gamma=120 degrees. A full set of X-ray diffraction data was collected to 2.5 A. Three heavy atom derivative data sets have been successfully obtained for Ace19 crystals and structural analysis is in progress.
  • Published In

    Keywords

  • Adhesins, Bacterial, Bacterial Proteins, Carrier Proteins, Crystallization, Crystallography, X-Ray, Enterococcus faecalis
  • Author List

  • Ponnuraj K; Xu Y; Moore D; Deivanayagam CCS; Boque L; Hook M; Narayana SVL
  • Start Page

  • 173
  • End Page

  • 176
  • Volume

  • 1596
  • Issue

  • 2