Search Results

You searched for all publications:

with publication states 'Published' 'Published (Approved)'

Search Again...

Author Name

Author Affiliation

Author ORCID

Title of Publication

DOI

Data DOI

Type of Publication (check all that apply) select all

Book Chapter

Conference Paper

Diamond Annual Review Highlight

Editors' Note

Journal Paper

Magazine Article

Poster

Report

Thesis

Title of Journal

Title of Conference

Peer Reviewed:

Yes No Either

Title of Magazine

Abstract

Keywords

Tags

Funding

Diamond Proposal Number

ISBN

BookChapter

Open Access:

Yes No Either

Published In or After Help

Published In or Before Help

Added In or After Help

Added In or Before Help

These results include publications that have not yet been reviewed and processed by Diamond Light Source. To view only processed publications click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

Exact matches
Related results

One item found (0 items not approved).1

Instruments / Technical Area	Publication Details	Published	Actions
Krios III-Titan Krios III at Diamond Krios IV-Titan Krios IV at Diamond	Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii Julius K. Demmer , Ben P. Phillips , O. Lisa Uhrig , Alain Filloux , Luke P. Allsopp , Maike Bublitz , Thomas Meier Science Advances 8 DOI: 10.1126/sciadv.abl5966 Diamond Proposal Number(s): [18659] Open Access Show Abstract ▼ Abstract: The global spread of multidrug-resistant Acinetobacter baumannii infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the F1Fo–adenosine 5′-triphosphate (ATP) synthase from A. baumannii in three distinct conformational states. The nucleotide-converting F1 subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded Fo complex, the structure shows unique structural adaptations along both the entry and exit pathways of the proton-conducting a-subunit. These features, absent in mitochondrial ATP synthases, represent attractive targets for the development of next-generation therapeutics that can act directly at the culmination of bioenergetics in this clinically relevant pathogen.	Feb 2022

Publications Database

Search Results

You searched for all publications:

Search Again...

Subject Areas (check all that apply) select all

Instruments used to collect data (check all that apply) select all

Collaborations involved (check all that apply) select all

Diamond Offline Facilities used

Relevant Technical Areas (check all that apply) select all

Menu for Anonymous User