English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Molecular architecture of Manduca sexta midgut V1 ATPase visualized by electron microscopy

Radermacher, M., Ruiz, T., Harvey, W. R., Wieczorek, H., & Grüber, G. (1999). Molecular architecture of Manduca sexta midgut V1 ATPase visualized by electron microscopy. FEBS Letters, 453(3), 383-386. doi:10.1016/S0014-5793(99)00739-5.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Radermacher, Michael1, Author           
Ruiz, Teresa1, Author           
Harvey, William R.2, Author
Wieczorek, Helmut3, Author
Grüber, Gerhard2, 3, Author
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Whitney Laboratory, University of Florida, St. Augustine, FL 32086, USA, ou_persistent22              
3Universität Osnabrück, Fachbereich Biologie/Chemie, D-49069 Osnabrück, Germany, ou_persistent22              

Content

show
hide
Free keywords: V1 ATPase; Electron microscopy; Image processing; Manduca sexta
 Abstract: The structure of the V1 ATPase from the tobacco hornworm Manduca sexta has been determined from electron micrographs of isolated, negatively stained specimens. The resulting images clearly show a pseudohexagonal arrangement of six equal-sized protein densities, presumably representing the three copies each of subunits A and B, which comprise the headpiece of the enzyme. A seventh density could be observed either centrally or asymmetrically to the hexamer. The maximum diameter of the V1 complex in the hexagonal projection is 13 nm with each of the six peripheral densities being 3–4 nm in diameter

Details

show
hide
Language(s): eng - English
 Dates: 1999-05-201999-04-041999-06-231999-06-25
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0014-5793(99)00739-5
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 453 (3) Sequence Number: - Start / End Page: 383 - 386 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501