Electron crystallography of ultrathin 3D protein crystals: Atomic model with charges

Koji Yonekura, Kazuyuki Kato, Mitsuo Ogasawara, Masahiro Tomita, Chikashi Toyoshima

Research output: Contribution to journalArticlepeer-review

106 Citations (Scopus)


Membrane proteins and macromolecular complexes often yield crystals too small or too thin for even the modern synchrotron X-ray beam. Electron crystallography could provide a powerful means for structure determination with such undersized crystals, as protein atoms diffract electrons four to five orders of magnitude more strongly than they do X-rays. Furthermore, as electron crystallography yields Coulomb potential maps rather than electron density maps, it could provide a unique method to visualize the charged states of amino acid residues and metals. Here we describe an attempt to develop a methodology for electron crystallography of ultrathin (only a few layers thick) 3D protein crystals and present the Coulomb potential maps at 3.4-Å and 3.2-Å resolution, respectively, obtained from Ca2+-ATPase and catalase crystals. These maps demonstrate that it is indeed possible to build atomic models from such crystals and even to determine the charged states of amino acid residues in the Ca2+-binding sites of Ca2+-ATPase and that of the iron atom in the heme in catalase.

Original languageEnglish
Pages (from-to)3368-3373
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number11
Publication statusPublished - 2015 Mar 17
Externally publishedYes


  • Ca-ATPase
  • Catalase
  • Coulomb potential
  • Electron crystallography
  • Protein crystal

ASJC Scopus subject areas

  • General


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