Imaging proteins at the single-molecule level

Longchamp, J.; Rauschenbach, S.; Abb, S.; Escher, C.; Latychevskaia, T.; Kern, K.; Fink, H.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Imaging proteins at the single-molecule level

MPS-Authors

/persons/resource/persons280418

Rauschenbach, S.
Department Nanoscale Science (Klaus Kern), Max Planck Institute for Solid State Research, Max Planck Society;

/persons/resource/persons280131

Kern, K.
Department Nanoscale Science (Klaus Kern), Max Planck Institute for Solid State Research, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Longchamp, J., Rauschenbach, S., Abb, S., Escher, C., Latychevskaia, T., Kern, K., et al. (2017). Imaging proteins at the single-molecule level. Proceedings of the National Academy of Sciences of the United States of America, 114(7), 1474-1479.

Cite as: https://hdl.handle.net/21.11116/0000-000E-CF8A-E

Abstract

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.