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  Crystallization and preliminary X-ray diffraction studies of the ∊ζ addiction system encoded by Streptococcus pyogenes plasmid pSM19035

Meinhart, A., Alings, C., Sträter, N., Camacho, A. G., Alonso, J. C., & Saenger, W. (2001). Crystallization and preliminary X-ray diffraction studies of the ∊ζ addiction system encoded by Streptococcus pyogenes plasmid pSM19035. Acta Crystallographica Section D: Structural Biology, 57(5), 745-747. doi:10.1107/S0907444901004176.

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ActaCrystD_57_2001_745.pdf (Any fulltext), 112KB
 
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 Creators:
Meinhart, Anton1, 2, Author           
Alings, Claudia, Author
Sträter, Norbert, Author
Camacho, Ana G., Author
Alonso, Juan C., Author
Saenger, Wolfram, Author
Affiliations:
1mRNA Processing, Max Planck Institute for Medical Research, Max Planck Society, ou_1497729              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: εζ toxin−antitoxin complex
 Abstract: The proteins encoded by the Streptococcus pyogenes broad-host range and low copy-number plasmid pSM19035 form a toxin–antitoxin module that secures stable maintenance by causing the death of plasmid-free segregants. The ∊ζ protein complex was crystallized in four different forms at pH 5.0 and pH 7.0 using the vapour-diffusion method with PEG 3350 and ethylene glycol as precipitants. Three of the crystal forms were obtained in the same droplet under identical conditions at pH 5.0. One form belongs to the enantiomorphic space groups P43212 or P41212. For the other two, the X-­ray reflection conditions match those of space group P212121, one representing a superlattice of the other. A crystal form growing at pH 7.0 also belongs to space group P212121, but there is no indication of a structural relationship to the other orthorhombic forms. Initially, the crystals diffracted to 2.9 Å resolution and diffracted to 1.95 Å after soaking at pH 7.0. A preparation of selenomethionyl ∊ζ protein complex yielded single crystals suitable for X-ray diffraction experiments using synchrotron sources.

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Language(s): eng - English
 Dates: 2001-02-012001-03-072001-05
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S0907444901004176
 Degree: -

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Title: Acta Crystallographica Section D: Structural Biology
  Abbreviation : Acta Cryst. D
Source Genre: Journal
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Publ. Info: Chester, England : International Union of Crystallography
Pages: - Volume / Issue: 57 (5) Sequence Number: - Start / End Page: 745 - 747 Identifier: ISSN: 2059-7983
CoNE: https://pure.mpg.de/cone/journals/resource/2059-7983