Crystallization of Hemoglobins II and III of the Symbiont-Harboring Clam Lucina pectinata

M. A. Doyle, Jacqueline Vitali, J. B. Wittenberg, S. N. Vinogradov, D. A. Walz, B. F.P. Edwards, P. D. Martin

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    Abstract

    Diffraction data to 2.7 A resolution were measured on crystals of the homotetramers of components II and III of the cytoplacmic hemoglobin of the symbiont-harboring clam Lucina pectinata. Even though the crystallization conditions are different and the sequence homology of the two hemoglobins is only 63%, the crystals are isomorphous to each other and to the heterotetramer Hb II/III, implying that the residues primarily involved in the intermolecular interactions and responsible for crystal cohesion may be invariant.

    Original languageAmerican English
    JournalActa Crystallographica Section D: Biological Crystallography
    VolumeD50
    DOIs
    StatePublished - Sep 1 1994

    Disciplines

    • Biochemistry
    • Biophysics

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