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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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Publisher copy:
10.1038/srep08773

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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
Language:
English
Keywords:
Pubs id:
pubs:509998
UUID:
uuid:07f86366-982e-4e88-834e-52fcc418bb6b
Local pid:
pubs:509998
Deposit date:
2018-03-26

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