Comparison of Molecular Packing between Two Kinds of Hen Egg-White Lysozyme Orthorhombic Crystals

DOI Web Site 24 References
  • AIBARA Shigeo
    Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • MIZUTANI Kimihiko
    Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • SUZUKI Atsuo
    Department of Biotechnology, Graduate School of Engineering, Nagoya University
  • HORIUCHI Hayato
    Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • HASHIMOTO Kazuhiko
    Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • YAMANE Takashi
    Department of Biotechnology, Graduate School of Engineering, Nagoya University

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The crystal packing of two orthorhombic crystal forms, Ⅰ and Ⅱ,of hen egg-white lysozyme(E.．C．３．２．１．１７，HEWL）that appeared at growth temperatures under 293K and 310K, respectively, was studied. The form I　crystal, whose crystal packing was newly investigated in this paper, was crystallized not only in a microgravity environment but also on Earth.The crystal packing of the space-grown crystals at 293K　proved to be very similar to those of the corresponding earth-grown form I　crystals at 277K and 293K, but it was significantly different from that of the from Ⅱcrystal grown at 310K. These two orthorhombic crystal forms had a common repeating unit consisting of two molecules, but the molecular arrangement of this unit differed substantially between the forms. Crystal in a microgravity field seems to grow by the same mechanism as the form I crystal grown on Earth. To explain the difference seen for the form Ⅱ crystals, we propose a molecular-growth mechanism for HEWL　orthorhombic crystals on the basis of the hydrophobic interaction. Further, we hypothesize that the protein molecules are incorporated into the crystal nuclei to complete the common molecular contact, and so the growth unit is a monomer.

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