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    Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):160-2. Epub 2001 Dec 21.

    Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli.

    Jormakka M, Törnroth S, Abramson J, Byrne B, Iwata S.

    Source

    Division of Biomedical Sciences, Imperial College, London SW7 2AZ, England.

    Abstract

    A membrane-protein complex, formate dehydrogenase-N from Escherichia coli, has been purified and crystallized. This molybdenum-containing enzyme, composed of alpha, beta and gamma subunits, is the major electron donor to the nitrate respiratory chain of E. coli. The formate dehydrogenase-N crystals belong to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 203 A. An asymmetric unit of the crystals is assumed to contain one formate dehydrogenase-N monomer (MW 170 kDa). One data set to 1.6 A resolution, with 342 711 independent observations (94.4% complete) and an R(merge) of 0.08, has been collected from a single crystal. This is the highest resolution data set reported for a membrane-protein complex to date.

    PMID:
    11752799
    [PubMed - indexed for MEDLINE]

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