Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa L-arginine deiminase

Yamina Oudjama, Catherine Tricot, Victor Stalon, Johan Wouters

    Research output: Contribution to journalArticle

    Abstract

    Pseudomonas aeruginosa L-arginine deiminase, an enzyme catalyzing the irreversible catabolism of arginine to citrulline, has been produced in selenomethionyl form. The protein was purified and crystallized by the sitting-drop vapour-diffusion method using a precipitant solution consisting of 55% MPD, 100 mM cacodylate pH 6.5, 20 mM MgCl2. Crystals display tetragonal symmetry (P41212 or P43212), with unit-cell parameters a = b = 106.0, c = 300.2 Å, and diffract to 2.7 Å. resolution. A complete MAD data set was collected to 3.2 Å resolution on beamline BM30 at ESRF.

    Original languageEnglish
    Pages (from-to)2150-2152
    Number of pages3
    JournalActa Crystallographica Section D: Biological Crystallography
    Volume58
    Issue number12
    DOIs
    Publication statusPublished - 1 Dec 2002

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