Abstract
The virion of filamentous bacterial viruses comprises a cylindrical protein shell of o.d. ∼60 Å and i.d. 20 Å, containing a single-stranded circular DNA molecule which has two oppositely directed but not base-paired strands extending the length of the virion. The assembly of the virion involves an intracellular prepackaging of the DNA with a viral DNA-binding protein which is then displaced by the coat protein as the growing virion crosses the bacterial membrane1. Studies of the virion by X-ray fibre diffraction show that the protein coat consists largely of α-helices oriented roughly parallel to the axis of the virion2,3. As the normal to a planar peptide tends to align normal to a magnetic field, it is possible to improve significantly the orientation of virions in fibres using a strong magnet4,5. The success of this technique with the Pf1 strain of virus led us to apply it to the better-known fd (f1, M13) strain. We report here new information about the arrangement of protein and DNA in the fd virion obtained from the improved diffraction pattern (Fig. 1).
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Banner, D., Nave, C. & Marvin, D. Structure of the protein and DNA in fd filamentous bacterial virus. Nature 289, 814–816 (1981). https://doi.org/10.1038/289814a0
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DOI: https://doi.org/10.1038/289814a0
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