Crystal packing in two pH-dependent crystal forms of rhamnogalacturonan acetylesterase

Anne Mølgaard, S. Larsen

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    The glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form was obtained at pH 5.0 and the trigonal crystal form at pH 4.5. In one case, the two crystal forms were found in the same drop at pH 4.7. The differences in crystal packing in the two crystal forms can be explained by the pH-dependent variation in the protonation state of the glutamic acid residues on the protein surface.
    Original languageEnglish
    JournalActa Crystallographica Section D
    Volume60
    Pages (from-to)472-478
    DOIs
    Publication statusPublished - 2004

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