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'The ribosome is a complex particle that makes the thousands of proteins that are required for the structure and function of each living cell. '1 'All three recipients [Venkatraman Ramakrishnan, Thomas Steitz, and Ada Yonath] of the 2009 Nobel Prize in Chemistry published papers on their award-winning work based on data collected at the U.S. Department of Energy's (DOE) Advanced Photon Source (APS) at Argonne National Laboratory.'2
[L]andmark progress in understanding the structure of the ribosome … [is also] based on data generated by a scientific technique called x-ray crystallography, performed at the National Synchrotron Light Source, operated by the U.S. Department of Energy's Brookhaven National Laboratory. …
The ribosome is the largest and most complex component of a cell to be successfully studied via x-ray crystallography. Researchers [including Venkatraman R. Ramakrishnan] from the University of Utah; the Medical Research Council Laboratory of Molecular Biology, Cambridge, England; and Brookhaven Lab presented a model of the small ribosomal subunit known as 30S, from the bacterium Thermus thermophilus. Yale University and Brookhaven researchers [including Thomas A. Steitz] reported on the structure of the large ribosomal subunit known as 50S, from the bacterium Haloarcula marismortui.'1
At Argonne, 'two separate groups resolved the structure of the small (30S) subunit at atomic-scale resolution. Ada Yonath led a group from the Weizmann Institute in Israel and the Max Planck Institute in Germany. The second group was led by Venki Ramakrishnan… .'3
'Knowledge of the ribosome's structure is helping scientists understand how many antibiotics attack certain parts, or functions, of the bacterial ribosome. Biologists in pharmaceutical and biotechnology companies will use this valuable information to develop new antibiotics to fight the growing problem of bacterial drug resistance.
… [R]esearchers also discovered that the ribosome's basic mechanisms for producing proteins are probably billions of years old because parts of these mechanisms are preserved among all organisms, from humans to bacteria.'3
For 'studies of the structure and function of the ribosome", the 2009 Nobel Prize in Chemistry has been awarded to Venkatraman Ramakrishnan, Thomas A. Steitz, and Ada E. Yonath.
1Edited excerpt from Landmark Progress in Understanding Ribosome Structure - Research Done at Brookhaven Lab's Light Source
Additional information about Venkatraman R. Ramakrishnan, Thomas Steitz, Ada Yonath, and ribosome is available in electronic documents and on the Web.
Neutron Scattering and the 30 S Ribosomal Subunit of E. Coli; Ramakrishnan, V.; DOE Technical Report; June 1982
Chemical and Physical Characterization of the Activation of Ribulosebiphosphate Carboxylase/Oxygenase; Ramakrishnan, V.; DOE Technical Report; August 1983
The Morphology of Emulsion Polymerized Latex Particles; Ramakrishnan, V.; DOE Technical Report; November 1987
Solving the Structure of Histone Acetyltransferase: Pushing the Limits of MAD; Ramakrishnan, V.; Biological Sciences, Page 1
Structure of the Large Ribosomal Subunit from H. marismortui at 5.5 Å Resolution; Steitz, T.A.; Biological Sciences, Page 15
Determination of the Atomic-Resolution Crystal Structure of the Large Subunit from the Ribosome of Haloarcula marismortui; Steitz, T. A., et. al.; nsls Newsletter, November 2000
The Atomic Resolution Crystal Structure of the Large Ribosomal Subunit from Haloarcula marismortui; Steitz, T.A., et. al.; NSLS Activity Report, 2000
Additional Web Pages:
Interview with Venkatraman Ramakrishnan, Thomas A. Steitz and Ada E. Yonath, December 6, 2009, nobelprize.org (video)
Nobel Lecture, December 8, 2009, nobelprize.org (video
Ribosome Redux at NSLS Crystallography Stations; November 1999 NSLS Newsletter, Second Article
Thomas A. Steitz:
Ada E. Yonath:
Nobel Lecture, December 8, 2009, nobelprize.org (video)
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