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  The structure of F−actin calculated from X−ray fibre diagrams and the 0.6nm crystal structure

Holmes, K. C., Popp, D., Gebhard, W., & Kabsch, W. (1989). The structure of F−actin calculated from X−ray fibre diagrams and the 0.6nm crystal structure. In U. Uaebi, & J. Engel (Eds.), Cytoskeletal and Extracellular Proteins (pp. 48-50). Heidelberg / Berlin: Springer.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-AE0C-8 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0000-B0D9-4
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Aebi_1989_CytoskeletalExtracellularProteins_48.pdf (beliebiger Volltext), 590KB
 
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https://link.springer.com/content/pdf/10.1007%2F978-3-642-73925-5.pdf (beliebiger Volltext)
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 Urheber:
Holmes, Kenneth C.1, 2, 3, Autor           
Popp, David, Autor
Gebhard, Werner2, 4, Autor           
Kabsch, Wolfgang2, 5, Autor           
Affiliations:
1Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society, ou_1497735              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              
4IT Group / Data processing, Max Planck Institute for Medical Research, Max Planck Society, ou_1497698              
5Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Zusammenfassung: The structure of the g-actin monomer complexed with DNaseI has been solved by x-ray crystallography to 0.45nm resolution, Fig.l (Kabsch, Mannherz, & Suck, 1985). In the following we describe the structure of f-actin arrived at by a search procedure: the structure obtained from crystallography at 0.6nm is placed in all possible orientations in the F-actin helix; the fibre diffraction pattern is computed from the resulting structure and compared with the x-ray diffraction data from orientated gels of F-actin (Popp, Lednev, & Jahn, 1986) measured to 0.8 nm resolution. This process yielded five possible solutions at low resolution (2.0nm) only one of which successfully refined to high resolution (0.8nm). A full account of this study is in preparation (Holmes, et al. 1989). The best of the five possible solutions resulting from the low resolution search is shown in Fig. 2. The (intensity) R-factor is 0.12. To refine at high resolution we adopted an iterative least squares procedure. However, no solution would refine satisfactorily. The resulting R-factors ranged from 0.37–0.45.

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Sprache(n): eng - English
 Datum: 1989
 Publikationsstatus: Erschienen
 Seiten: 3
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Interne Begutachtung
 Identifikatoren: DOI: 10.1007/978-3-642-73925-5_8
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Titel: Cytoskeletal and Extracellular Proteins
  Alternativer Titel : Springer Series in Biophysics, 3
Genre der Quelle: Buch
 Urheber:
Uaebi, U., Autor
Engel, J., Autor
Uaebi, U., Herausgeber
Engel, J., Herausgeber
Affiliations:
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Ort, Verlag, Ausgabe: Heidelberg / Berlin : Springer
Seiten: - Band / Heft: - Artikelnummer: - Start- / Endseite: 48 - 50 Identifikator: ISBN: 978-3-642-73927-9
ISBN: 978-3-642-73925-5