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Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase

Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_916146808

Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase

About this item

Full title

Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2011-12, Vol.481 (7380), p.214-218

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Insights into the rotary mechanism of the
Thermus thermophilus
ATP synthase are obtained using electron cryomicroscopy to determine its three-dimensional structure calculated to subnanometre resolution.
Structure of a rotary ATP synthase
In this paper, the authors present the high-resolution structure of an H
+
-driven ATP synthas...

Alternative Titles

Full title

Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_916146808

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_916146808

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature10699

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