Ribosomal crystallography: From poorly diffracting microcrystals to high-resolution structures

Marco Gluehmann, Raz Zarivach, Anat Bashan, Joerg Harms, Frank Schluenzen, Heike Bartels, Ilana Agmon, Gabriel Rosenblum, Marta Pioletti, Tamar Auerbach, Horacio Avila, Harly A.S. Hansen, François Franceschi, Ada Yonath

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

The cellular organelles translating the genetic code into proteins, the ribosomes, are large, asymmetric, flexible, and unstable ribonucleoprotein assemblies, hence they are difficult to crystallize. Despite two decades of intensive effort and thorough searches for suitable sources, so far only three crystal types have yielded high-resolution structures: two large subunits (from an archaean and from a mesophilic eubacterium) and one thermophilic small subunit. These structures have added to our understanding of decoding, have revealed dynamic aspects of the biosynthetic process, and have indicated the strategies adopted by ribosomes for interacting between themselves as well as with inhibitors, factors and substrates.

Original languageEnglish
Pages (from-to)292-302
Number of pages11
JournalMethods
Volume25
Issue number3
DOIs
StatePublished - 1 Jan 2001
Externally publishedYes

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