The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)

Olofsson, A. ; Hebert, H. ; Thelestam, M.

Amsterdam : Elsevier
ISSN:
0014-5793
Keywords:
Image processing ; Perfringolysin O, Electron microscopy
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Physics
Type of Medium:
Electronic Resource
URL:
_version_ 1798290828922191872
autor Olofsson, A.
Hebert, H.
Thelestam, M.
autorsonst Olofsson, A.
Hebert, H.
Thelestam, M.
book_url http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80050-5
datenlieferant nat_lic_papers
fussnote The cytolysin Perfringolysin O was applied to lipid layers and the obtained ring-shaped oligomers analyzed by electron microscopy and image processing. The final result shows the periodic repeat of 2.4 nm along the outer rim of the ring. The asymmetric protein unit, corresponding to one monomer, spans the ring from the convex to the concave surface. It shows a clear protein peak close to the outer radius and less density in the middle of the oligomer. The number of monomers in the average ring is 50, and the inner radius of the aggregate is approximately 15 nm.
hauptsatz hsatz_simple
identnr NLZ173302203
issn 0014-5793
journal_name FEBS Letters
materialart 1
package_name Elsevier
publikationsort Amsterdam
publisher Elsevier
reference 319 (1993), S. 125-127
schlagwort Image processing
Perfringolysin O, Electron microscopy
search_space articles
shingle_author_1 Olofsson, A.
Hebert, H.
Thelestam, M.
shingle_author_2 Olofsson, A.
Hebert, H.
Thelestam, M.
shingle_author_3 Olofsson, A.
Hebert, H.
Thelestam, M.
shingle_author_4 Olofsson, A.
Hebert, H.
Thelestam, M.
shingle_catch_all_1 Olofsson, A.
Hebert, H.
Thelestam, M.
The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
Image processing
Perfringolysin O, Electron microscopy
Image processing
Perfringolysin O, Electron microscopy
0014-5793
00145793
Elsevier
shingle_catch_all_2 Olofsson, A.
Hebert, H.
Thelestam, M.
The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
Image processing
Perfringolysin O, Electron microscopy
Image processing
Perfringolysin O, Electron microscopy
0014-5793
00145793
Elsevier
shingle_catch_all_3 Olofsson, A.
Hebert, H.
Thelestam, M.
The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
Image processing
Perfringolysin O, Electron microscopy
Image processing
Perfringolysin O, Electron microscopy
0014-5793
00145793
Elsevier
shingle_catch_all_4 Olofsson, A.
Hebert, H.
Thelestam, M.
The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
Image processing
Perfringolysin O, Electron microscopy
Image processing
Perfringolysin O, Electron microscopy
0014-5793
00145793
Elsevier
shingle_title_1 The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
shingle_title_2 The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
shingle_title_3 The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
shingle_title_4 The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
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source_archive Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
timestamp 2024-05-06T08:22:56.957Z
titel The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
titel_suche The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
The cytolysin Perfringolysin O was applied to lipid layers and the obtained ring-shaped oligomers analyzed by electron microscopy and image processing. The final result shows the periodic repeat of 2.4 nm along the outer rim of the ring. The asymmetric protein unit, corresponding to one monomer, spans the ring from the convex to the concave surface. It shows a clear protein peak close to the outer radius and less density in the middle of the oligomer. The number of monomers in the average ring is 50, and the inner radius of the aggregate is approximately 15 nm.
topic W
V
U
uid nat_lic_papers_NLZ173302203