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Current state of the structural analysis of the actin: DNase I complex

MPG-Autoren
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Kabsch,  Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Mannherz,  Hans Georg
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://link.springer.com/content/pdf/10.1007%2F978-3-642-73925-5.pdf
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https://doi.org/10.1007/978-3-642-73925-5_7
(beliebiger Volltext)

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Zitation

Kabsch, W., Pai, E. F., Mannherz, H. G., & Suck, D. (1989). Current state of the structural analysis of the actin: DNase I complex. In U. Aebi, & J. Engel (Eds.), Cytoskeletal and Extracellular Proteins (pp. 42-47). Heidelberg / Berlin: Springer.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-ADD6-6
Zusammenfassung
The complex between rabbit skeletal muscle actin and bovine pancreatic DNase I (Lazarides & Lindberg, 1974) can be crystallized in three different forms. The x-ray structure of the orthorhombic form III has been solved to a resolution of 0.6nm (Suck, Kabsch & Mannherz, 1981). More recently the resolution has been increased to 0.45nm and the actin molecule has been unambigously identified in the map (Kabsch, Mannherz & Suck, 1985). This identification was derived from knowledge of the DNase I atomic structure (Suck, Oefner & Kabsch, 1984). In addition, only one combination of actin and DNase I density was found which is common to both the monoclinic (form II) and the orthorhombic (form III) crystals. It was concluded that this unique combination must represent the complex as found in solution.