Impact of natural variation in bacterial F17G adhesins on crystallization behaviour

Lieven Buts, Adinda Wellens, Inge Van Molle, Lode Wyns, Remy Loris, Martina Lahmann, Stefan Oscarson, Henri De Greve, Julie Bouckaert

    Research output: Contribution to journalArticle

    10 Citations (Scopus)


    Since the introduction of structural genomics, the protein has been recognized as the most important variable in crystallization. Recent strategies to modify a protein to improve crystal quality have included rationally engineered point mutations, truncations, deletions and fusions. Five naturally occurring variants, differing in 1-18 amino acids, of the 177-residue lectin domain of the F17G fimbrial adhesin were expressed and purified in identical ways. For four out of the five variants crystals were obtained, mostly in non-isomorphous space groups, with diffraction limits ranging between 2.4 and 1.1 Å resolution. A comparative analysis of the crystal-packing contacts revealed that the variable amino acids are often involved in lattice contacts and a single amino-acid substitution can suffice to radically change crystal packing. A statistical approach proved reliable to estimate the compatibilities of the variant sequences with the observed crystal forms. In conclusion, natural variation, universally present within prokaryotic species, is a valuable genetic resource that can be favourably employed to enhance the crystallization success rate with considerably less effort than other strategies.
    Original languageEnglish
    Pages (from-to)1149-1159
    Number of pages11
    JournalActa Crystallographica Section D
    Publication statusPublished - 2005


    • adhesin
    • lectin
    • structural biology
    • protein-carbohydrate interactions


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