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

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.

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Aebi_1989_CytoskeletalExtracellularProteins_42.pdf (Any fulltext), 967KB
 
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 Creators:
Kabsch, Wolfgang1, 2, Author           
Pai, Emil F., Author
Mannherz, Hans Georg1, Author           
Suck, Dietrich, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: Polypeptide; Methylmercury
 Abstract: 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.

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Language(s): eng - English
 Dates: 1989
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Cytoskeletal and Extracellular Proteins
  Alternative Title : Springer Series in Biophysics, 3
Source Genre: Book
 Creator(s):
Aebi, U., Editor
Engel, J., Editor
Affiliations:
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Publ. Info: Heidelberg / Berlin : Springer
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 42 - 47 Identifier: ISBN: 978-3-642-73927-9
ISBN: 978-3-642-73925-5