Protein Crystallography and Structural Biology. Hot 3D Structures of Biological Macromolecules. Structure Analysis of Macrophage Migration Inhibitory Factor.

  • SUZUKI Mamoru
    Photon Factory, National Laboratory for High Energy Physics
  • SUGIMOTO Hiroshi
    Division of Biological Sciences, Graduate School of Science, Hokkaido University
  • NAKAGAWA Atsushi
    Division of Biological Sciences, Graduate School of Science, Hokkaido University
  • TANAKA Isao
    Division of Biological Sciences, Graduate School of Science, Hokkaido University

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  • タンパク質結晶学と構造生物学 新しいタンパク質立体構造 マクロファージ遊走阻止因子 セレノメチオニンを使ったMAD法による解析例
  • マクロファージ ユウソウ ソシ インシ セレノメチオニン オ ツカッタ MAD

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Abstract

Structure of macrophage migration inhibitory factor has been determined by the method of multiwavelength anomalous diffraction (MAD) with the use of synchrotron data from a crystal of the selenomethionyl protein. The protein contains three methionines in a single polypeptide chain of 114 amino residues. In the analysis, we prepared a series of selenomethionyl proteins by site-directed mutagenesis. The structure was solved using the crystal which contains only one methionine (therefore one Se) per single polypeptide chain.

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