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

Karthe Ponnuraj, Yi Xu, Dwight Moore, Champion C.S. Deivanayagam, Lluis Boque, Magnus Hook, Sthanam V.L. Narayana

Research output: Contribution to journalArticle

10 Scopus citations

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 Å data set has been collected on the orthorhombic crystal form with unit cell parameters a=38.43 b=48.91 and c=83.73 Å. Ace40 was crystallized in the trigonal space group P3121 or P3221 with unit cell parameters a=b=80.24, c=105.91 Å; α=β=90 and γ=120°. A full set of X-ray diffraction data was collected to 2.5 Å. Three heavy atom derivative data sets have been successfully obtained for Ace19 crystals and structural analysis is in progress.

Original languageEnglish (US)
Pages (from-to)173-176
Number of pages4
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1596
Issue number2
DOIs
StatePublished - Apr 29 2002

Keywords

  • Ace
  • Collagen binding
  • Crystallization
  • Enterococcus faecalis
  • Microbial surface component recognizing adhesive matrix molecule

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

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