English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits

MPS-Authors
/persons/resource/persons160227

Mühleip,  Alexander W.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137764

Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137632

Davies,  Karen M.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Mühleip, A. W., Dewar, C. E., Schnaufer, A., Kühlbrandt, W., & Davies, K. M. (2017). In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits. Proceedings of the National Academy of Sciences of the United States of America, 114(5), 992-997. doi:10.1073/pnas.1612386114.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-A131-5
Abstract
There is no abstract available