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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

Authors


More from this funder
Name:
NIGMS NIH HHS
Grant:
R01GM66223
R01 GM066223
More from this funder
Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/I004831/1
BB/L01985X/1
More from this funder
Name:
Biotechnology & Biological Sciences Research Council
Grant:
BB/I004831/1
BB/L01985X/1
Publisher:
Springer Nature
Journal:
Scientific Reports More from this journal
Volume:
5
Issue:
1
Pages:
8773
Publication date:
2015-03-10
Acceptance date:
2015-01-29
DOI:
ISSN:
2045-2322
Pmid:
25753753
Language:
English
Keywords:
Pubs id:
pubs:509998
UUID:
uuid:07f86366-982e-4e88-834e-52fcc418bb6b
Local pid:
pubs:509998
Source identifiers:
509998
Deposit date:
2018-03-26

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