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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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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-AE0C-8 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-B0D9-4
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Aebi_1989_CytoskeletalExtracellularProteins_48.pdf (Any fulltext), 590KB
 
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 Creators:
Holmes, Kenneth C.1, 2, 3, Author           
Popp, David, Author
Gebhard, Werner2, 4, Author           
Kabsch, Wolfgang2, 5, Author           
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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 Abstract: 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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Language(s): eng - English
 Dates: 1989
 Publication Status: Issued
 Pages: 3
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 Rev. Type: Internal
 Identifiers: DOI: 10.1007/978-3-642-73925-5_8
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Title: Cytoskeletal and Extracellular Proteins
  Alternative Title : Springer Series in Biophysics, 3
Source Genre: Book
 Creator(s):
Uaebi, U., Author
Engel, J., Author
Uaebi, U., Editor
Engel, J., Editor
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Publ. Info: Heidelberg / Berlin : Springer
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 48 - 50 Identifier: ISBN: 978-3-642-73927-9
ISBN: 978-3-642-73925-5