Ada Yonath

Ada E. Yonath
Born	Ada Lifshitz 22 6, 1939
Birthplace	Jerusalem, Mandatory Palestine
Nationality	Israeli
Occupation	Crystallographer, professor
Employer	Weizmann Institute of Science
Known for	Pioneering work on ribosome structure; cryo bio-crystallography
Education	Ph.D. in X-ray crystallography (Weizmann Institute of Science)
Awards	Nobel Prize in Chemistry (2009), Israel Prize (2002), Wolf Prize in Chemistry (2007)
Website	[http://www.weizmann.ac.il/sb/faculty_pages/Yonath/home.html Official site]

Ada E. Yonath (Template:Lang-he; born Ada Lifshitz, 22 June 1939) is an Israeli crystallographer and Nobel laureate best known for her groundbreaking research into the three-dimensional structure of the ribosome, the molecular machine within cells responsible for translating genetic information into proteins. Born in Jerusalem during the period of the British Mandate for Palestine, Yonath pursued what many of her contemporaries considered a near-impossible scientific challenge—mapping the atomic structure of one of the largest and most complex biological assemblies ever studied by X-ray crystallography. In 2009, she was awarded the Nobel Prize in Chemistry, jointly with Venkatraman Ramakrishnan and Thomas A. Steitz, for studies on the structure and function of the ribosome. In receiving the prize, Yonath became the first Israeli woman to win a Nobel Prize, the first woman from the Middle East to receive a Nobel in the sciences, and the first woman in 45 years to win the Nobel Prize for Chemistry. She serves as director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly at the Weizmann Institute of Science.

Early Life

Ada Yonath was born Ada Lifshitz on 22 June 1939 in Jerusalem, in what was then Mandatory Palestine. She grew up in modest circumstances. Her parents were Zionist immigrants who had moved to Palestine from Poland. Her father was a rabbi and the family lived in the Geula neighborhood of Jerusalem, where financial hardship was a constant reality.

Despite the family's economic struggles, Yonath displayed an early intellectual curiosity about the natural world. In a 2018 interview, she recalled that as a child she had a deeply inquisitive nature, though she noted, "I never wanted to be a scientist." Nevertheless, her natural inclination toward experimentation was evident from a young age. As a child, she famously attempted to measure the height of the ceiling in her family's apartment by stacking furniture, an effort that ended with a fall and a broken arm—an early anecdote that would become illustrative of her determination and willingness to take on seemingly impossible challenges.

Her father died when she was eleven years old, a loss that compounded the family's financial difficulties. Following his death, the family relocated to Tel Aviv, where Yonath continued her schooling. Despite the hardships she faced, she excelled academically and developed a growing interest in science during her secondary education. The move to Tel Aviv also provided access to better educational opportunities, and Yonath took advantage of these to pursue her scientific interests.

Education

Yonath attended high school in Tel Aviv and subsequently enrolled at the Hebrew University of Jerusalem, where she studied chemistry and later earned a master's degree in biochemistry. She then pursued doctoral studies at the Weizmann Institute of Science in Rehovot, Israel, where she completed her Ph.D. in X-ray crystallography under the supervision of Wolfie Traub. Her doctoral research introduced her to the techniques of crystallography that would become central to her life's work.

Following her doctorate, Yonath undertook postdoctoral research in the United States, working with F. Albert Cotton, who served as one of her doctoral advisors, and expanding her expertise in structural biology. These formative years of training in both Israel and the United States equipped Yonath with the technical skills and theoretical knowledge that would later enable her to pursue the structural determination of the ribosome.

Career

Early Research and the Ribosome Challenge

Upon completing her postdoctoral work, Yonath returned to Israel and joined the faculty of the Weizmann Institute of Science, where she would spend the bulk of her career. She also held a position at the University of Chicago. In the late 1970s and early 1980s, Yonath embarked on what would become her defining scientific endeavor: determining the three-dimensional atomic structure of the ribosome through X-ray crystallography.

The ribosome is a massive molecular complex found in all living cells, responsible for translating the genetic instructions encoded in messenger RNA into proteins—the molecules that carry out virtually all cellular functions. Proteins are the most essential building blocks for life; organisms would not be able to breathe, eat, or fight infection without the proteins produced by ribosomes, including hemoglobin, digestion enzymes, and immune system components. Understanding the ribosome's structure at atomic resolution was therefore considered one of the most important and challenging problems in structural biology.

At the time Yonath began her work, most scientists considered the crystallization of ribosomes to be an impossible task. Ribosomes are enormous by molecular standards—composed of hundreds of thousands of atoms—and their inherent flexibility and complexity made them exceedingly difficult to crystallize, a prerequisite for X-ray crystallographic analysis. Yonath took on this challenge despite widespread skepticism from the scientific community. As the Nobel Prize organization noted, she "took on a challenge that others considered hopeless."

Development of Cryo Bio-Crystallography

One of Yonath's most significant methodological contributions was the development and refinement of cryo bio-crystallography, a technique involving the cooling of biological crystals to extremely low temperatures in order to minimize radiation damage during X-ray data collection. This innovation was instrumental in making it possible to collect usable diffraction data from ribosomal crystals, which were especially sensitive to the intense X-ray beams required for structural analysis.

The technique drew inspiration from an unexpected source. Yonath has recounted how she was influenced by observations of how polar bears' ribosomes could remain organized even in a hibernation state, which suggested that cooling might help preserve the structural integrity of ribosomal crystals during experimentation. This method, along with other technical innovations she introduced, gradually enabled the production of increasingly well-ordered ribosomal crystals and the collection of diffraction data of sufficient quality to begin solving the structure.

The work was painstaking and extended over more than two decades. During this period, Yonath faced not only the inherent scientific difficulties of the project but also personal setbacks, including a serious concussion sustained in a bicycle accident. Rather than halting her research, the accident and subsequent recovery period inadvertently contributed to new insights that advanced her work.

Mapping the Ribosome Structure

Yonath's research utilized advanced synchrotron radiation facilities, including those operated by the United States Department of Energy, to collect the diffraction data necessary for structural determination. The use of these powerful X-ray sources was essential for resolving the positions of hundreds of thousands of atoms within the ribosomal complex.

By the late 1990s and early 2000s, Yonath and her team at the Weizmann Institute achieved a series of breakthroughs, producing increasingly detailed maps of both the large and small subunits of the ribosome. The 2009 Nobel Prize in Chemistry cited the achievement of the "detailed mapping of the ribosome—the cell's own protein factory" as the basis for the award. The structural maps revealed how the ribosome reads mRNA and assembles amino acids into proteins, providing fundamental insights into one of the most essential processes in biology.

These structural revelations had profound implications not only for basic science but also for medicine. The ribosome is the target of many antibiotic drugs. By revealing the precise atomic structure of the ribosome, Yonath's work provided a detailed understanding of how antibiotics bind to and inhibit bacterial ribosomes. This knowledge opened new avenues for the design of more effective antibiotics—a matter of growing urgency given the worldwide rise of antibiotic-resistant bacteria.

Ongoing Research and Antibiotic Development

Following the Nobel Prize, Yonath continued her research at the Weizmann Institute, where she serves as director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly. Her ongoing work has focused on exploiting the structural knowledge of the ribosome to develop novel antibiotics that can overcome bacterial resistance mechanisms. This research program builds directly on the atomic-resolution maps of antibiotic binding sites on the ribosome that her earlier work produced.

Yonath has been described as "one of the most prolific scientists in the world" for the breadth and impact of her contributions to structural biology and crystallography. Her research continues to explore fundamental questions about how the ribosome functions and how its activity can be modulated by drugs.

Contributions to Crystallography

In addition to her ribosome-specific achievements, Yonath's career has contributed substantially to the broader field of crystallography. In a 2014 interview marking the International Year of Crystallography, she reflected on how the discipline had evolved during her career and emphasized the importance of crystallographic methods in understanding biological systems at the molecular level. Her development of cryo bio-crystallography techniques has had applications far beyond ribosome research, influencing structural studies of many other large and fragile biological molecules.

Personal Life

Ada Yonath has one daughter, Hagit Yonath, who is herself a scientist. Yonath has spoken publicly about the challenges of balancing a demanding scientific career with family responsibilities, particularly as a single mother in a field dominated by men during much of her career.

In interviews, Yonath has revealed aspects of her personality that contrast with the stereotypical image of a laboratory scientist. In her 2018 Chemistry World interview, she discussed her childhood curiosity and the unexpected paths that led her to science, noting that her original aspirations were not specifically oriented toward a scientific career. She has also spoken about her love of reading and the role of imagination in scientific discovery.

Yonath has been noted for her sense of humor and directness. In various public appearances following her Nobel Prize, she has discussed the personal costs of fame, including the disruption to her research schedule caused by the demands of public lectures, interviews, and ceremonial obligations.

Recognition

Ada Yonath has received numerous awards and honors throughout her career, reflecting the significance of her contributions to science.

Her most prominent recognition is the Nobel Prize in Chemistry, awarded in 2009 jointly with Venkatraman Ramakrishnan and Thomas A. Steitz "for studies of the structure and function of the ribosome." The prize recognized work that spanned more than two decades and resulted in the first atomic-resolution structural maps of the ribosome.

Prior to the Nobel Prize, Yonath received the Israel Prize in 2002, one of the highest honors awarded by the State of Israel, recognizing her contributions to chemistry and scientific research. In 2007, she was awarded the Wolf Prize in Chemistry, another prestigious international science award.

In 2008, Yonath received a Life Work Prize for women in science from the Israeli Ministry of Foreign Affairs, recognizing her sustained contributions to the field.

Yonath has also been recognized by the Albert Einstein World Award of Science, presented by the World Cultural Council.

She has received honorary degrees from numerous institutions worldwide. In 2015, the University of Warwick awarded her an honorary degree in recognition of her scientific achievements. In 2018, Carnegie Mellon University invited her as a keynote speaker and honorary degree recipient at its commencement ceremonies, describing her as "one of the most prolific scientists in the world."

In 2014, Yonath was appointed to the Pontifical Academy of Sciences by Pope Francis.

Legacy

Ada Yonath's work on the ribosome constitutes one of the landmark achievements of structural biology in the late twentieth and early twenty-first centuries. Her determination of the atomic structure of the ribosome provided the scientific community with an unprecedented understanding of how genetic information is translated into the proteins that sustain life. This work has had lasting implications for both basic biological research and the development of medical therapeutics, particularly in the field of antibiotic design.

Her development of cryo bio-crystallography techniques has had a transformative effect on the broader field of structural biology, enabling the study of large and fragile molecular complexes that were previously inaccessible to high-resolution structural analysis. These methods continue to be used in laboratories around the world and have contributed to structural studies of many biological systems beyond the ribosome.

As the first Israeli woman and the first woman from the Middle East to receive a Nobel Prize in the sciences, Yonath has become a prominent figure in discussions about gender representation in the scientific community. Her career, marked by decades of persistence in the face of skepticism and technical obstacles, has served as an example for subsequent generations of scientists. Her story—from a childhood of economic hardship in Jerusalem to the Nobel stage in Stockholm—illustrates the capacity of sustained scientific inquiry to yield transformative knowledge about the fundamental processes of life.

Yonath continues her research at the Weizmann Institute of Science, where she remains active in the investigation of ribosome structure and the development of new antibiotic strategies to combat drug-resistant bacteria.