Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: myofilament lengths

H. Sosa, D. Popp, G. Ouyang, H. E. Huxley

Research output: Contribution to journalArticlepeer-review

98 Scopus citations


We have set up a system to rapidly freeze muscle fibers during contraction to investigate by electron microscopy the ultrastructure of active muscles. Glycerinated fiber bundles of rabbit psoas muscles were frozen in conditions of rigor, relaxation, isometric contraction, and active shortening. Freezing was carried out by plunging the bundles into liquid ethane. The frozen bundles were then freeze-substituted, plastic-embedded, and sectioned for electron microscopic observation. X-ray diffraction patterns of the embedded bundles and optical diffraction patterns of the micrographs resemble the x-ray diffraction patterns of unfixed muscles, showing the ability of the method to preserve the muscle ultrastructure. In the optical diffraction patterns layer lines up to 1/5.9 nm-1 were observed. Using this method we have investigated the myofilament lengths and concluded that there are no major changes in length in either the actin or the myosin filaments under any of the conditions explored.

Original languageEnglish (US)
Pages (from-to)283-292
Number of pages10
JournalBiophysical journal
Issue number1
StatePublished - 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics


Dive into the research topics of 'Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: myofilament lengths'. Together they form a unique fingerprint.

Cite this