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

doi:10.1016/S0167-4838(01)00328-4

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 journal › Article › peer-review

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 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	https://doi.org/10.1016/S0167-4838(01)00328-4
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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10.1016/S0167-4838(01)00328-4

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Ponnuraj, K., Xu, Y., Moore, D., Deivanayagam, C. C. S., Boque, L., Hook, M., & Narayana, S. V. L. (2002). Crystallization and preliminary X-ray crystallographic analysis of Ace: A collagen-binding MSCRAMM from Enterococcus faecalis. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1596(2), 173-176. https://doi.org/10.1016/S0167-4838(01)00328-4

Ponnuraj, K, Xu, Y, Moore, D, Deivanayagam, CCS, Boque, L, Hook, M & Narayana, SVL 2002, 'Crystallization and preliminary X-ray crystallographic analysis of Ace: A collagen-binding MSCRAMM from Enterococcus faecalis', Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, vol. 1596, no. 2, pp. 173-176. https://doi.org/10.1016/S0167-4838(01)00328-4

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

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

keywords = "Ace, Collagen binding, Crystallization, Enterococcus faecalis, Microbial surface component recognizing adhesive matrix molecule",

author = "Karthe Ponnuraj and Yi Xu and Dwight Moore and Deivanayagam, {Champion C.S.} and Lluis Boque and Magnus Hook and Narayana, {Sthanam V.L.}",

year = "2002",

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doi = "10.1016/S0167-4838(01)00328-4",

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AU - Ponnuraj, Karthe

AU - Xu, Yi

AU - Moore, Dwight

AU - Deivanayagam, Champion C.S.

AU - Boque, Lluis

AU - Hook, Magnus

AU - Narayana, Sthanam V.L.

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N2 - 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.

AB - 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.

KW - Ace

KW - Collagen binding

KW - Crystallization

KW - Enterococcus faecalis

KW - Microbial surface component recognizing adhesive matrix molecule

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JO - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

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

Abstract

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