Ribosomal crystallography: from poorly diffracting microcrystals to high-resolution structures.

M Gluehmann; R Zarivach; A Bashan; J Harms; F Schluenzen; H Bartels; I Agmon; G Rosenblum; M Pioletti; T Auerbach; H Avila; H A Hansen; F Franceschi; A Yonath

doi:10.1006/meth.2001.1241

PubMed · 11860283

Ribosomal crystallography: from poorly diffracting microcrystals to high-resolution structures.

M Gluehmann·R Zarivach·A Bashan·J Harms·F Schluenzen·H Bartels·I Agmon·G Rosenblum·M Pioletti·T Auerbach·H Avila·H A Hansen·F Franceschi·A Yonath

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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.

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Archaea Bacterial Proteins Crystallography, X-Ray Microscopy, Electron Models, Molecular Protein Binding Protein Conformation Protein Structure, Tertiary RNA Ribosomes X-Ray Diffraction Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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M Gluehmann, R Zarivach, A Bashan, J Harms, F Schluenzen, H Bartels, I Agmon, G Rosenblum, M Pioletti, T Auerbach, H Avila, H A Hansen, F Franceschi, A Yonath. 2001. Ribosomal crystallography: from poorly diffracting microcrystals to high-resolution structures.. https://doi.org/10.1006/meth.2001.1241

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