Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 11, Pages 3368-3373Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1500724112
Keywords
electron crystallography; protein crystal; Coulomb potential; Ca2+-ATPase; catalase
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Funding
- Japan Science and Technology Agency SENTAN program
- Japan Society for the Promotion of Science [24657111]
- Ministry of Education, Culture Sports, Science and Technology of Japan
- Grants-in-Aid for Scientific Research [24657111, 23000014] Funding Source: KAKEN
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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-angstrom and 3.2-angstrom 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.
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