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The Ribosome - Three-Dimensional Structure and Ligand-Binding Studies

Published online by Cambridge University Press:  02 July 2020

J. Frank ,
P. Penczek ,
A. Malhotra ,
I. Gabashvili ,
R. Grassucci ,
A. Heagle ,
S. Srivastava ,
N. Burkhardt ,
R. Jünemann  and
K.H. Nierhaus
...Show all authors
J. Frank
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509 Department of Biomedical Sciences, State University of New York at Albany
P. Penczek
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509 Department of Biomedical Sciences, State University of New York at Albany
A. Malhotra
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509
I. Gabashvili
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509
R. Grassucci
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509
A. Heagle
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509
S. Srivastava
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509
N. Burkhardt
Affiliation:
Max-Planck-Institut fur Molekulare Genetik, Ihnestrasse 73, D-14195Berlin, Germany
R. Jünemann
Affiliation:
Max-Planck-Institut fur Molekulare Genetik, Ihnestrasse 73, D-14195Berlin, Germany
K.H. Nierhaus
Affiliation:
Max-Planck-Institut fur Molekulare Genetik, Ihnestrasse 73, D-14195Berlin, Germany
R.K. Agrawal
Affiliation:
Wadsworth Center, New York State Department of Health, Albany, New York12201-0509
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Extract

To date, cryo-electron microscopy has become the most successful technique for exploring the structure of the ribosome and for studying binding positions of its various ligands, with the resolution slowly extending toward 10 Å. Obstacles in the attempts to improve resolution are the limited stability and coherence of the electron microscope, the statistics of data collection, and the conformational heterogeneity of the specimen. The last factor in this list proved to be the reason why it has been difficult to go past 18-20 Å with many specimens despite the use of state-of-the-art electron microscopes and inclusion of tens of thousand of projections.

A breakthrough has been achieved with a protein synthesis initiation-like complex in which mRNA and fMet-tRNA is bound to the E. coli ribosome. The high occupancy and extraordinary conformational homogeneity of this specimen has enabled us to reach a resolution of 15 Å.

Type
Chambers and Channels: Functional Connections in Multiprotein Complexes Studied by Single Chambers and Channels
Information
Microscopy and Microanalysis , Volume 4 , Issue S2: Proceedings: Microscopy & Microanalysis '98, Microscopy Society of America 56th Annual Meeting, Microbeam Analysis Society 32nd Annual Meeting, Atlanta, Georgia July 12-16, 1998 , July 1998 , pp. 962 - 963
Copyright
Copyright © Microscopy Society of America

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References

References:

1.Frank, J. et al., Nature 376(1995)441.CrossRefGoogle Scholar
2.Stark, H. et al., Structure 3(1995)815.CrossRefGoogle Scholar
3.Agrawal, R.K. et al., Science 271(1996)1000.CrossRefGoogle Scholar
4.Stark, H. et al., Cell 88(1997)19.CrossRefGoogle Scholar
5.Malhotra, A. et al., (1998)submitted.Google Scholar
6.Radermacher, M. et al., EMBO J. 6(1987)1107.CrossRefGoogle Scholar
7.Agrawal, R.K. et al., (1998)submitted.Google Scholar
8.Beckmann, R. et al., Science 278(1997)2123.CrossRefGoogle Scholar
9. Supported, in part, by NIH R37 GM29169 and R01 GM55440.Google Scholar