Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea

L K Skov, Osman Asghar Mirza, A Henriksen, G Potocki de Montalk, M Remaud-Simeon, P Sarcabal, R M Willemot, P Monsan, M Gajhede

    28 Citations (Scopus)

    Abstract

    Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.
    Original languageEnglish
    JournalActa Crystallographica. Section D: Biological Crystallography
    Volume56
    Issue numberPt 2
    Pages (from-to)203-5
    Number of pages3
    ISSN0907-4449
    Publication statusPublished - Feb 2000

    Keywords

    • Bacterial Proteins
    • Circular Dichroism
    • Crystallization
    • Crystallography, X-Ray
    • Escherichia coli
    • Glucosyltransferases
    • Neisseria
    • Recombinant Proteins

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