Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana

Massant, Jan; Peeters, Eveline; Charlier, Daniel; Maes, Dominique

doi:10.1107/S1744309105039618

Title: Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana

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Abstract

The arginine repressor of the hyperthermophile T. neapolitana was crystallized with and without its corepressor arginine. Both crystals diffracted to high resolution and belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with similar unit-cell parameters. The arginine repressor of Thermotoga neapolitana (ArgRTnp) is a member of the family of multifunctional bacterial arginine repressors involved in the regulation of arginine metabolism. This hyperthermophilic repressor shows unique DNA-binding features that distinguish it from its homologues. ArgRTnp exists as a homotrimeric protein that assembles into hexamers at higher protein concentrations and/or in the presence of arginine. ArgRTnp was crystallized with and without its corepressor arginine using the hanging-drop vapour-diffusion method. Crystals of the aporepressor diffracted to a resolution of 2.1 Å and belong to the orthorhombic P2{sub 1}2{sub 1}2{sub 1} space group, with unit-cell parameters a = 117.73, b = 134.15, c = 139.31 Å. Crystals of the repressor in the presence of its corepressor arginine diffracted to a resolution of 2.4 Å and belong to the same space group, with similar unit-cell parameters.

Authors:

Massant, Jan; Peeters, Eveline; Charlier, Daniel ^[1]; Maes, Dominique ^[2]

Laboratorium voor Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels (Belgium)
Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel and Vlaams Interuniversitair Instituut voor Biotechnologie, Pleinlaan 2, B-1050 Brussels (Belgium)

Publication Date:: Sun Jan 01 00:00:00 EST 2006

OSTI Identifier:: 22356244

Resource Type:: Journal Article

Journal Name:: Acta Crystallographica. Section F

Additional Journal Information:: Journal Volume: 62; Journal Issue: Pt 1; Other Information: PMCID: PMC2150929; PMID: 16511254; PUBLISHER-ID: gx5074; OAI: oai:pubmedcentral.nih.gov:2150929; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091

Country of Publication:: United Kingdom

Language:: English

Subject:: 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ARGININE; CRYSTALLIZATION; CRYSTALS; DIFFUSION; DNA; PROTEINS; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats


                    Massant, Jan, Peeters, Eveline, Charlier, Daniel, Maes, Dominique, and Laboratorium voor Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels. Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana.  United Kingdom: N. p., 2006. 
        Web.  doi:10.1107/S1744309105039618.

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                    Massant, Jan, Peeters, Eveline, Charlier, Daniel, Maes, Dominique, & Laboratorium voor Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels. Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana.  United Kingdom.  https://doi.org/10.1107/S1744309105039618

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                    Massant, Jan, Peeters, Eveline, Charlier, Daniel, Maes, Dominique, and Laboratorium voor Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels. 2006.  
        "Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana".  United Kingdom.  https://doi.org/10.1107/S1744309105039618.

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@article{osti_22356244,

  title        = {Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana},

  author       = {Massant, Jan and Peeters, Eveline and Charlier, Daniel and Maes, Dominique and Laboratorium voor Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels},

  abstractNote = {The arginine repressor of the hyperthermophile T. neapolitana was crystallized with and without its corepressor arginine. Both crystals diffracted to high resolution and belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with similar unit-cell parameters. The arginine repressor of Thermotoga neapolitana (ArgRTnp) is a member of the family of multifunctional bacterial arginine repressors involved in the regulation of arginine metabolism. This hyperthermophilic repressor shows unique DNA-binding features that distinguish it from its homologues. ArgRTnp exists as a homotrimeric protein that assembles into hexamers at higher protein concentrations and/or in the presence of arginine. ArgRTnp was crystallized with and without its corepressor arginine using the hanging-drop vapour-diffusion method. Crystals of the aporepressor diffracted to a resolution of 2.1 Å and belong to the orthorhombic P2{sub 1}2{sub 1}2{sub 1} space group, with unit-cell parameters a = 117.73, b = 134.15, c = 139.31 Å. Crystals of the repressor in the presence of its corepressor arginine diffracted to a resolution of 2.4 Å and belong to the same space group, with similar unit-cell parameters.},

  doi          = {10.1107/S1744309105039618},

  url          = {https://www.osti.gov/biblio/22356244},
  journal      = {Acta Crystallographica. Section F},

  issn         = {1744-3091},

  number       = Pt 1,

  volume       = 62,

  place        = {United Kingdom},

  year         = {Sun Jan 01 00:00:00 EST 2006},

  month        = {Sun Jan 01 00:00:00 EST 2006}

}

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