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    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):128-32. Epub 2009 Jan 31.

    Preliminary structural investigations of the Eut-L shell protein of the ethanolamine ammonia-lyase metabolosome of Escherichia coli.

    Nikolakakis K, Ohtaki A, Newton K, Chworos A, Sagermann M.

    Source

    Department of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, California 93106-9510, USA.

    Abstract

    The ethanolamine ammonia-lyase microcompartment is composed of five different shell proteins that have been proposed to assemble into symmetrically shaped polyhedral particles of varying sizes. Here, preliminary X-ray analysis of crystals of the bacterial microcompartment shell protein Eut-L from Escherichia coli is reported. Cloning, overexpression and purification resulted in highly pure protein that crystallized readily under many different conditions. In all cases the protein forms thin hexagonal plate-shaped crystals belonging to space group P3 that are of unusually high stability against different solvent conditions. The crystals diffracted to a resolution of 2.0 A using synchrotron radiation but proved to be radiation-sensitive. Preparations of heavy-atom-derivatized crystals for use in determining the three-dimensional structure are under way.

    PMID:
    19194002
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2635865
    Free PMC Article

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