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The positions of the N-terminus and residue 68 in tobacco mosaic virus

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Mandelkow,  Eckhard
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Arbeitsgruppe Zytoskelett, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93463

Holmes,  Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/002228367490148X/pdf?md5=7a09ee6de55207bfdd8da1c691077df0&pid=1-s2.0-002228367490148X-main.pdf
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https://doi.org/10.1016/0022-2836(74)90148-X
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Citation

Mandelkow, E., & Holmes, K. C. (1974). The positions of the N-terminus and residue 68 in tobacco mosaic virus. Journal of Molecular Biology (London), 87(2), 265-273. doi:10.1016/0022-2836(74)90148-X.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-B17C-7
Abstract
Specific chemical modifications of the tobacco mosaic virus coat protein lead to new heavy-atom derivatives. They can be used for the determination of phases in the isomorphous replacement method, but more important they are necessary as markers if one wants to trace the polypeptide chain through an electron density map of limited resolution (10 Å). In addition to the positions of two residues known from previous work, two more residues out of the 158 have now been located in three dimensions. The N-terminus is at the outside of the particle (r = 88 Å), and Lys-68 lies at a radius of 72 Å.