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Imaging proteins at the single-molecule level.

  • Longchamp JN Physics Department of the University of Zurich, CH-8057 Zurich, Switzerland; longchamp@physik.uzh.ch k.kern@fkf.mpg.de hwfink@physik.uzh.ch.
  • Rauschenbach S Max Planck Institute for Solid State Research, DE-70569 Stuttgart, Germany.
  • Abb S Max Planck Institute for Solid State Research, DE-70569 Stuttgart, Germany.
  • Escher C Physics Department of the University of Zurich, CH-8057 Zurich, Switzerland.
  • Latychevskaia T Physics Department of the University of Zurich, CH-8057 Zurich, Switzerland.
  • Kern K Max Planck Institute for Solid State Research, DE-70569 Stuttgart, Germany; longchamp@physik.uzh.ch k.kern@fkf.mpg.de hwfink@physik.uzh.ch.
  • Fink HW Physics Department of the University of Zurich, CH-8057 Zurich, Switzerland; longchamp@physik.uzh.ch k.kern@fkf.mpg.de hwfink@physik.uzh.ch.
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  • 2017-01-15
Published in:
  • Proceedings of the National Academy of Sciences of the United States of America. - 2017
low-energy electron holography
microscopy
preparative mass spectrometry
single protein imaging
structural biology
Animals
Cattle
Cytochromes c
Electrons
Graphite
Hemoglobins
Holography
Proteins
Serum Albumin, Bovine
Single Molecule Imaging
Spectrometry, Mass, Electrospray Ionization
Static Electricity
Vacuum
English Imaging single proteins has been a long-standing ambition for advancing various fields in natural science, as for instance structural biology, biophysics, and molecular nanotechnology. In particular, revealing the distinct conformations of an individual protein is of utmost importance. Here, we show the imaging of individual proteins and protein complexes by low-energy electron holography. Samples of individual proteins and protein complexes on ultraclean freestanding graphene were prepared by soft-landing electrospray ion beam deposition, which allows chemical- and conformational-specific selection and gentle deposition. Low-energy electrons do not induce radiation damage, which enables acquiring subnanometer resolution images of individual proteins (cytochrome C and BSA) as well as of protein complexes (hemoglobin), which are not the result of an averaging process.
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  • English
Open access status
bronze
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https://sonar.ch/global/documents/259490
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