Home LiteratureArticle Details
PMID: 6190821 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A consistent picture of the actin filament related to the orientation of the actin molecule.

The Journal of cell biology ·Vol. 97 ·No. 1 ·1983-07-00 ·Pages 264-9

Fowler WE, Aebi U

Abstract

We show that freeze-dried actin filaments which have been rotary shadowed with a light coat of platinum appear very similar in morphology and width to negatively-stained filaments. The addition of a thicker coat of platinum to such preparations gives the actin filaments a different morphology and width, which are similar to those of the rotary-shadowed, quick-frozen filaments described by Heuser and Kirschner (J. Cell Biol. 1980, 86:212-234). The consistent view of the actin filament presented here, particularly its 7-8-nm width, can be interpreted in terms of the overall orientation of the actin subunit in the actin filament.

MeSH Terms
Actins Freeze Drying Macromolecular Substances Microscopy, Electron Models, Molecular Staining and Labeling
Chemicals
Actins Macromolecular Substances
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fowler W E
Aebi U
References (18)
18 references, click to expand
  1. The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy.
    J Ultrastruct Res. 1968 Sep;24(5):454-64 PMID: 5751523
  2. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments.
    J Mol Biol. 1970 Jun 14;50(2):279-95 PMID: 5476917
  3. Regulation of skeletal muscle contraction. II. Structural studies of the interaction of the tropomyosin-troponin complex with actin.
    J Mol Biol. 1972 Dec 30;72(3):619-32 PMID: 4349760
  4. Electron microscopy of the stacked disk aggregate of tobacco mosaic virus protein. II. The influence of electron irradiation of the stain distribution.
    J Mol Biol. 1974 Aug 25;87(4):657-70 PMID: 4139268
  5. Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin I complex.
    J Mol Biol. 1975 Apr 25;93(4):477-97 PMID: 1142432
  6. Freeze drying and shadowing a two-dimensional periodic specimen.
    J Ultrastruct Res. 1977 Apr;59(1):76-86 PMID: 66324
  7. Structure of actin-containing filaments from two types of non-muscle cells.
    J Mol Biol. 1977 Jul 15;113(4):679-95 PMID: 561192
  8. Apparent holes in rotary shadowed proteins: dependence on angle of shadowing and replica thickness.
    J Microsc. 1979 Nov;117(2):313-5 PMID: 399302
  9. Filament organization revealed in platinum replicas of freeze-dried cytoskeletons.
    J Cell Biol. 1980 Jul;86(1):212-34 PMID: 6893451
  10. Freeze-drying specimens for electron microscopy.
    J Ultrastruct Res. 1980 Sep;72(3):380-4 PMID: 6107386
  11. Structure of F-actin needles from extracts of sea urchin oocytes.
    J Mol Biol. 1981 Feb 15;146(1):77-99 PMID: 6894946
  12. Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution.
    Proc Natl Acad Sci U S A. 1981 Jul;78(7):4319-23 PMID: 6270671
  13. Crystalline actin sheets: their structure and polymorphism.
    J Cell Biol. 1981 Nov;91(2 Pt 1):340-51 PMID: 7309785
  14. F-actin is a helix with a random variable twist.
    Nature. 1982 Jul 8;298(5870):131-5 PMID: 7201078
  15. Polymorphism of actin paracrystals induced by polylysine.
    J Cell Biol. 1982 May;93(2):452-8 PMID: 7096448
  16. Role of fimbrin and villin in determining the interfilament distances of actin bundles.
    Nature. 1983 Jan 20;301(5897):209-14 PMID: 6823301
  17. Crystallographic studies of the chicken gizzard G-actin X DNase I complex at 5A resolution.
    J Biochem. 1983 Jan;93(1):299-302 PMID: 6221013
  18. F-ACTIN IS A RIGHT-HANDED HELIX.
    J Mol Biol. 1965 May;12:302-3 PMID: 14343294
Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1983-07-00
Pages
264-9
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2112490
Subset
IM
Grants
NIGMS NIH HHS · GM-27765 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com