Crystallization of <i>Escherichia coli</i> ribosomes

Wittmann, H. G.; Müssig, J.; Piefke, Jutta; Gewitz, H.S.; Rheinberger, Hans‐Jörg; Yonath, Ada

doi:10.1016/0014-5793(82)80739-4

Cited by 55 publications

(13 citation statements)

References 10 publications

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“…Such analysis is limited by the inherent lower resolution induced by the embedding process, by the uncer tainty regarding the exact sectioning direction, and by the unknown factors governing the stain distribution within the particle. However, despite these shortcomings, useful information could be extracted concerning the pack ing of the crystals of the 70S ribosome from E. coli (41) and the stain distributi0 f/. within the 50S subunits from B. stearothermophilus.…”

Section: Electron Microscopy Of Sectioned Three-dimensional Crystalsmentioning

confidence: 99%

Approaching Atomic Resolution in Crystallography of Ribosomes

Yonath¹

1992

Annu. Rev. Biophys. Biomol. Struct.

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Section: Electron Microscopy Of Sectioned Three-dimensional Crystalsmentioning

confidence: 99%

Approaching Atomic Resolution in Crystallography of Ribosomes

Yonath¹

1992

Annu. Rev. Biophys. Biomol. Struct.

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“…As for the spherical viruses, in all the structures solved at high resolution the RNA part is disordered and cannot be seen on the electron density maps. 8 -10 The field is now expanding rapidly and recently the small ribosomal subunit 4 and the complete ribosome 5 have been crystallized as well as complexes between restriction endonucleases and DNA fragments. 6 • 7 The crystals described in the following pages are made of a tRNA with its cognate aminoacyl-tRNA synthetase.…”

mentioning

confidence: 99%

Yeast tRNA^Asp-Aspartyl-tRNA Synthetase: The Crystalline Complex

Moras

Lorber

Romby

et al. 1983

Journal of Biomolecular Structure and Dynamics

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Aspartyl-tRNA synthetase from yeast, a dimer of molecular weight 125,000 and its cognate tRNA (Mr = 24,160) were co-crystallized using ammonium sulfate as precipitant agent. The presence in the crystals of both components in the two-to-one stoichiometric ratio was demonstrated by electrophoresis, biological activity assays and crystallographic data. Crystals belong to the cubic space group I432 with cell parameter of 354 A and one complex particle per asymmetric unit. The solvent content of about 78% is favorable for a low resolution structural investigation. By exchanging H2O for D2O in mother liquors, advantage can be taken from contrast variation techniques with neutron radiations. Diffraction data to 20 A resolution were measured at five different contrasts, two of them being close to the theoretical matching point of RNA and protein in the presence of ammonium sulfate. The experimental extinction of the diffracted signal was observed to be close to 36% D2O, significantly different from the predicted value of 41%. The phenomenon can be explained by the existence of a large interface region between the two tRNAs and the enzyme. These parts of the molecules are hidden from the solvent and their protons are less easily exchangeable. Accessibility studies toward chemicals of tRNAAsp in solution and in the presence of synthetase are in agreement with such a model.

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“…However, it took another decade before single crystals of much better behaving ribosomes from E. coli were reported [170]. The crystals of complete ribosomes were not amenable to crystallographic studies at that time and, therefore, the individual subunits of E. coli and Bacillus stearothermophilus ribosomes were crystallized separately [171].…”

Section: Ribosome: the Translation Machinementioning

confidence: 99%

A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits

2014

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As a contribution to the celebration of the year 2014, declared by the United Nations to be ‘The International Year of Crystallography’, the FEBS Journal is dedicating this issue to papers showcasing the intimate union between macromolecular crystallography and structural biology, both in historical perspective and in current research. Instead of a formal editorial piece, by way of introduction, this review discusses the most important, often iconic, achievements of crystallographers that led to major advances in our understanding of the structure and function of biological macromolecules. We identified at least 42 scientists who received Nobel Prizes in Physics, Chemistry or Medicine for their contributions that included the use of X‐rays or neutrons and crystallography, including 24 who made seminal discoveries in macromolecular sciences. Our spotlight is mostly, but not only, on the recipients of this most prestigious scientific honor, presented in approximately chronological order. As a summary of the review, we attempt to construct a genealogy tree of the principal lineages of protein crystallography, leading from the founding members to the present generation.

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Crystallization of Escherichia coli ribosomes

Cited by 55 publications

References 10 publications

Approaching Atomic Resolution in Crystallography of Ribosomes

Approaching Atomic Resolution in Crystallography of Ribosomes

Yeast tRNA^Asp-Aspartyl-tRNA Synthetase: The Crystalline Complex

A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits

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Crystallization of Escherichia coli ribosomes

Cited by 55 publications

References 10 publications

Approaching Atomic Resolution in Crystallography of Ribosomes

Approaching Atomic Resolution in Crystallography of Ribosomes

Yeast tRNAAsp-Aspartyl-tRNA Synthetase: The Crystalline Complex

A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits

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Product

Resources

About

Yeast tRNA^Asp-Aspartyl-tRNA Synthetase: The Crystalline Complex