Structure of a beheaded 30 S ribosomal subunit from Thermus thermophilus

Igor Serdyuk, Andrey Ulitin, Igor Kolesnikov, Victor Vasiliev, Victor Aksenov, Guiseppe Zaccai, Dmitri Svergun, Michael Kozin, Regine Willumeit

Research output: Article


The 22 S ribonucleoproten particles containing the 5' (body) and the central (platform) domains of the Thermus thermophilus 30 S subunit has been studied by sedimentation, neutron scattering and electron microscopy. The RNP particles have been obtained by oligonucleotide-directed cleavage of 16 S RNA with ribonulease H in the region of the 900th nucleotide of the protein-deficient derivatives of the 30 S subunits. It is shown that these RNP particles are very compact, though their form and dimensions differ slightly from those expected from the electron microscopy model of the 30 S subunit beheaded by computer simulation. The particles are subdivided into two structural domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30 S subunit. Electron microscopy demonstrates that the mutual arrangement of domains in the RNP particles is not strictly fixed suggesting that interaction with the third domain of the 30 S subunit is a requisite for their correct fitting.

Original languageEnglish
Pages (from-to)633-639
Number of pages7
JournalJournal of molecular biology
Issue number3
Publication statusPublished - szept. 24 1999

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Serdyuk, I., Ulitin, A., Kolesnikov, I., Vasiliev, V., Aksenov, V., Zaccai, G., Svergun, D., Kozin, M., & Willumeit, R. (1999). Structure of a beheaded 30 S ribosomal subunit from Thermus thermophilus. Journal of molecular biology, 292(3), 633-639.