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

Biochim Biophys Acta. 2002 Apr 29;1596(2):173-6. doi: 10.1016/s0167-4838(01)00328-4.

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.

Publication types

  • Comparative Study

MeSH terms

  • Adhesins, Bacterial*
  • Bacterial Proteins / chemistry*
  • Carrier Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Enterococcus faecalis / chemistry
  • Enterococcus faecalis / metabolism*

Substances

  • Ace protein, Enterococcus
  • Adhesins, Bacterial
  • Bacterial Proteins
  • Carrier Proteins
  • adhesin, Staphylococcus aureus