Literature DB >> 1715910

Circular harmonic averaging of rotary-shadowed and negatively stained creatine kinase macromolecules.

H Winkler1, H Gross, T Schnyder, W Kunath.   

Abstract

The structure of mitochondrial creatine kinase is investigated by high-resolution shadowing at very low temperature and conventional negative staining. The electron microscopic images are analyzed with circular harmonic averaging, a method suited for the processing of single molecules. The rotational alignment and averaging is performed with the circular harmonic components, which allows data compression and several steps of noise reduction to be carried out within the averaging procedure. In addition, the symmetry can be deduced. For the mitochondrial creatine kinase, a fourfold symmetry is found that is compatible with the biochemical and biophysical characterization of the molecule.

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Year:  1991        PMID: 1715910     DOI: 10.1002/jemt.1060180207

Source DB:  PubMed          Journal:  J Electron Microsc Tech        ISSN: 0741-0581


  2 in total

Review 1.  Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis.

Authors:  T Wallimann; M Wyss; D Brdiczka; K Nicolay; H M Eppenberger
Journal:  Biochem J       Date:  1992-01-01       Impact factor: 3.857

Review 2.  The structure of mitochondrial creatine kinase and its membrane binding properties.

Authors:  T Schnyder; M Rojo; R Furter; T Wallimann
Journal:  Mol Cell Biochem       Date:  1994 Apr-May       Impact factor: 3.396

  2 in total

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