Journal article
Imaging proteins at the single-molecule level
- 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.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
-
-
(Preview, Accepted manuscript, pdf, 1.5MB, Terms of use)
-
- Publisher copy:
- 10.1073/pnas.1614519114
Authors
+ Swiss National Science Foundation (Schweizerische Nationalfonds)
More from this funder
- Grant:
- PZ00P2_148084
- 200021_150049
- Publisher:
- National Academy of Sciences
- Journal:
- Proceedings of the National Academy of Sciences of the United States of America More from this journal
- Volume:
- 114
- Issue:
- 7
- Pages:
- 1474-1479
- Publication date:
- 2017-02-14
- DOI:
- EISSN:
-
1091-6490
- ISSN:
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0027-8424
- Pmid:
-
28087691
- Language:
-
English
- Keywords:
- Pubs id:
-
pubs:729764
- UUID:
-
uuid:758c9ea3-26a9-4656-b21e-628de7621c82
- Local pid:
-
pubs:729764
- Source identifiers:
-
729764
- Deposit date:
-
2018-01-05
- ARK identifier:
Terms of use
- Copyright holder:
- © Longchamp, et al 2017
- Copyright date:
- 2017
- Notes:
- This is the author accepted manuscript following peer review version of the article. The final version is available online from National Academy of Sciences at: 10.1073/pnas.1614519114
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