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Crystal structure of a mutant of archaeal ribosomal protein L1 from Methanococcus jannaschii

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Abstract

The crystal structure of a mutant of archaeal ribosomal protein L1 from Methanococcus jannaschii with the deletion of a nonconserved positively charged cluster consisting of eight C-terminal amino acid residues is determined by the molecular replacement method at 1.75 Å resolution. This mutant is shown to form more stable and ordered crystals belonging to a space group other than that of the wild-type protein crystals. The positively charged C-terminal region has only a slight effect on the interaction between protein L1 and RNA molecules. Hence, this mutant can be used to prepare protein-RNA complexes and obtain their crystals.

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Authors and Affiliations

  1. Institute of Protein Research, Russian Academy of Sciences, Institutskaya ul. 4, Pushchino, Moscow oblast, 142290, Russia

    A. V. Sarskikh, A. G. Gabdulkhakov, O. S. Kostareva, A. A. Shklyaeva & S. V. Tishchenko

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  1. A. V. Sarskikh
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  2. A. G. Gabdulkhakov
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  3. O. S. Kostareva
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  4. A. A. Shklyaeva
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  5. S. V. Tishchenko
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Correspondence to S. V. Tishchenko.

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Original Russian Text © A.V. Sarskikh, A.G. Gabdulkhakov, O.S. Kostareva, A.A. Shklyaeva, S.V. Tishchenko, 2014, published in Kristallografiya, 2014, Vol. 59, No. 3, pp. 438–442.

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Sarskikh, A.V., Gabdulkhakov, A.G., Kostareva, O.S. et al. Crystal structure of a mutant of archaeal ribosomal protein L1 from Methanococcus jannaschii . Crystallogr. Rep. 59, 394–398 (2014). https://doi.org/10.1134/S1063774514030158

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  • DOI: https://doi.org/10.1134/S1063774514030158

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