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 language | English (US) |
|---|---|
| Pages (from-to) | 173-176 |
| Number of pages | 4 |
| Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
| Volume | 1596 |
| Issue number | 2 |
| DOIs | |
| State | Published - 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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