Journal article
Comparison between single-molecule and X-ray crystallography data on yeast F1-ATPase
- Abstract:
-
Single molecule studies in recent decades have elucidated the full chemo-mechanical cycle of F1-ATPase, mostly based on F1 from thermophilic bacteria. In contrast, high-resolution crystal structures are only available for mitochondrial F1. Here we present high resolution single molecule rotational data on F1 from Saccharomyces cerevisiae, obtained using new high throughput detection and analysis tools. Rotational data are presented for the wild type mitochondrial enzyme, a “liver” isoform, an...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Funding
Bibliographic Details
- Publisher:
- Springer Nature Publisher's website
- Journal:
- Scientific Reports Journal website
- Volume:
- 5
- Issue:
- 1
- Pages:
- 8773
- Publication date:
- 2015-03-10
- Acceptance date:
- 2015-01-29
- DOI:
- ISSN:
-
2045-2322
- Pmid:
-
25753753
- Source identifiers:
-
509998
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:509998
- UUID:
-
uuid:07f86366-982e-4e88-834e-52fcc418bb6b
- Local pid:
- pubs:509998
- Deposit date:
- 2018-03-26
Terms of use
- Copyright holder:
- Bradley C Steel et al
- Copyright date:
- 2015
- Notes:
- This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/>
- Licence:
- CC Attribution (CC BY)
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