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virus' protective coat

The Cornell High Energy Synchrotron Source (CHESS) congratulates Ada E. Yonath (Weitzman Institute, Israel), Thomas A Steitz (Yale University, USA, and Venkatraman Ramakrishnan (MRC Laboratory of Molecular Biology, UK) for receipt of the 2009 Nobel Prize in Chemistry for their pioneering studies elucidating the structure and function of "one of life's core processes: the ribosome's translation of DNA information into life". The Royal Swedish Academy noted the importance of synchrotron x-ray crystallography in providing atomic-level structural information of the ribosome. These scientists led independent efforts to discover the three-dimensional positions of hundreds of thousands of individual atoms that together comprise the ribosome.

Maps with atomic details are extremely useful and their published work shows how a variety of antibiotics bind to ribosomes. "These models are now used by scientists in order to develop new antibiotics, directly assisting the saving of lives and decreasing humanity's suffering," the Academy announcement said. Many antibiotics cure diseases by blocking the function of bacterial ribosomes, they continued; "Without functional ribosomes, bacteria cannot survive. This is why ribosomes are such an important target for new antibiotics".

The Royal Academy’s scientific background release (see link [1] below) refers to the early work by Yonath as “In summary, Ada Yonath’s work throughout the 1980s has been instrumental for obtaining the robust and well diffracting ribosome crystals that eventually led to high resolution structures of the two ribosomal subunits.” They go on to point out that a full visualization would take another ten years, culminating in seminal publications in year 2000, and would involve two other main players, including Thomas Steitz and Venkatraman Ramakrishnan.

Keith Moffat, founder in 1982 of the macromolecular crystallography resource at CHESS (MacCHESS) recalls that Yonath was a frequent user of CHESS starting in the mid-1980s, when she was struggling to collect x-ray diffraction data from her new crystals of ribosomes. “We gave her a lot of help” he adds. “As a user with a particularly challenging problem, she both needed it and welcomed it. The award is for her enormous contributions to the determination of their structure; she richly deserves it".

These were formative years both for Yonath’s pioneering work on the structure of the ribosome and for the development of new x-ray technologies and methods that are now parts of the well-established and enormously productive field of “protein crystallography". Yonath was among the first scientists to use the newly constructed “F1” station, the first experimental station at CHESS intentionally designed and dedicated to protein crystallography. From today’s perspective it is clear that these scientists were true pioneers who had to invent solutions to difficult crystallographic problems. This time period saw the development of cryocrystallography. At the time, crystals were mounted on thin glass plates, whose use was pioneered by Yonath and colleague Håkon Hope [2]. The plates were made by blowing large glass bubbles and breaking them into little pieces. Yonath provided CHESS with an Oxford cryosystem for her experiments. Even after MacCHESS acquired its own cryosystems from Molecular Structures Corp., Yonath preferred to use her own, causing the staff worries whenever the Oxford system, with its fragile glass transfer line, had to be taken out of storage, checked to see that it was in good working condition, and mounted on the beamline for her experiments.

Data from many synchrotron sources were used by the Nobel recipients to perform their work. CHESS contributed to Yonath’s ribosomal work in several important ways. The Royal Swedish Academy of Sciences scientific background paper to the award [1] refers to the progressive improvement of crystals over the years that diffracted to higher and higher resolution. Many of Yonath’s visits to CHESS were to examine these crystals, e.g. [3], culminating in some of the first low-resolution structures of ribosomal subunits [4] [5]. The Royal Academy also noted technological developments necessary to the eventual success of Yonath, Steitz, and Ramakrishnan. Several of these involved CHESS/MacCHESS, including the development of methods to cryoprotect crystals against radiation damage [2] [6], the development of CCD detectors applied to macromolecular crystallography (first introduced at MacCHESS in the early 1990’s [7]), and anomalous diffraction methods of phasing structures [8].

This is the third time in seven years that the Royal Swedish Academy has awarded Nobel chemistry prizes for work based on synchrotron crystallography. In 2003 Rod MacKinnon (Rockefeller University, USA) shared the prize with Peter Agre (Johns Hopkins University, USA). MacKinnon’s 1998 solution of the structure of potassium channel, using data acquired at CHESS, was followed by a series of structural revelations of ion channels using data from CHESS and several other synchrotron sources. In 2006 Roger D. Kornberg (Stanford University, USA) was awarded the prize for studies of the molecular basis of eukaryotic transcription, largely involving data acquired at the Stanford Synchrotron Radiation Laboratory.

 

[1] Royal Swedish Academy of Sciences scientific background paper to the 2009 Nobel Chemistry award: http://nobelprize.org/nobel_prizes/chemistry/laureates/2009/cheadv09.pdf

[2] H. Hope, F. Frolow, K. von Bohlen I. Makowski, C. Kratky, Y. Halfon, H. Danz, P. Webster, K.S. Bartels, H.G. Wittmann, and A. Yonath; “Cryocrystallography of Ribosomal Particles”, Acta Cryst B45, 190-199 (1989)

[3] I. Makowski, F. Frolow, M. Saper, M. Shoham, H.G. Wittmann, and A. Yonath; “Single Crystals of Large Ribosomal Particles from Halobacteriun Marismortui Diffract to 6 Å”, J. Mol. Biol. 193, 819-822 (1987)

[4] A. Tocilj, F. Schluenzen, H.A.S. Hansen, A. Bashan, D. Janell, M. Gluehmann, H. Bartels, J. Harms., A. Agmon, F. Franceschi, and A. Yonath; “The Small Ribosomal Subunit from Thermus thermophilus at 4.5A Resolution: pattern fitting and the identification of functional sites", PNAS 96, 14252-14257 (1999)

[5] F. Schluenzen, A. Tocilj, R. Zarivach, J. Harms, M. Glueman, D. Janell, A. Basha, H. Bartels, I. Agmon, F. Franceschi, and A. Yonath; “Structure of Functionally Activated Small Ribosomal Subunit at 3.3A Resolution", Cell 102, 615-623 (2000)

[6] T-Y Teng; “Mounting of Crystals for Macromolecular Crystallography in a Free-standing Thin Film", J. Appl. Cryst. 23, 387-391 (1990)

[7] R.L. Walter, D.J. Thiel, S. Barna, M.W. Tate, M.E. Wall, E.F. Eikenberry, S.M. Gruner, S.E. Ealick; “High-resolution Macromolecular Structure Determination using CCD Detectors and Synchrotron Radiation", Structure 3, 835-844 (1995)

[8] W.A. Hendrickson; “Determination of Macromolecular Structures From Anomalous Diffraction of Synchrotron Radiation", Science 254, 51-58 (1991)

 

CHESS is a synchrotron user facility supported by the U.S. National Science Foundation through the Division of Materials Research, with supplementary support from the National Institute of General Medical Sciences, National Institutes of Health. MacCHESS is a Research Resource Supported by the National Institute of Research Resources, National Institutes of Health.

 

10/09/2009