Crystallography

Not just a Nobel Prize: The long road Ada Yonath took to turning the ribosome into the key to understanding antibiotics

Not just a Nobel Prize: The long road Ada Yonath took to turning the ribosome into the key to understanding antibiotics

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A day after the news of her death was published, Weizmann Institute materials highlight the scientific legacy she left behind: decades of struggle with a problem that was considered almost insoluble, development of crystallographic methods, deciphering the ribosome, and laying the foundation for understanding
Prof. Ada Yonath, Nobel Prize laureate in Chemistry, passes away at age 87

Prof. Ada Yonath, Nobel Prize laureate in Chemistry, passes away at age 87

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Prof. Ada Yonath of the Weizmann Institute, who deciphered the structure of the ribosome and won the Nobel Prize in Chemistry in 2009, passed away on August 31, 2026. Over decades of research, she persisted on questions that were considered almost unanswerable.
Technion President Prof. Uri Sivan confers the honorary degree on Prof. Ada Yonat. Photo: Rami Shlush, Technion Spokesperson

The Technion awarded an honorary doctorate to writer David Grossman and Nobel laureate Prof. Ada Yonat

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Prof. Ada Yonat from the Weizmann Institute of Science, winner of the 2009 Nobel Prize in Chemistry, received an honorary doctorate "in recognition of her pioneering contribution to the research of the ribosome - the universal complex for translating genetic information into proteins
Rosalind Franklin during her stay in France. Photo: from Wikipedia

New findings on Rosalind Franklin's role in discovering the structure of DNA

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An article published in Nature details Franklin's part in discovering the "backbone" of the DNA molecule. However, due to the competition between the groups, she avoided publishing a large part of them herself, as well as Watson and Crick
For the first time, the mechanism that creates an electrical pulse in a nerve cell has been documented. Prof. Igor Shapiro, Hebrew University

For the first time, the mechanism that creates an electrical pulse in a nerve cell was documented

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Figure - on the left: the atomic structure of the protein segment that forms the biofilm fibers in E. coli and Salmonella. This structure is very similar to the structures of amyloid fibers associated with Alzheimer's disease, and this structural similarity led to the idea of ​​damaging the bacterial biofilm fibers using the substances developed against Alzheimer's fibers. Above (in black and white): images taken with an electron microscope. On the left are visible fibers that are formed by the bacterial protein and are used to build the biofilm; On the right is shown the damage to fiber formation as a result of the addition of the substance that opens Alzheimer's fibers (ANK6) Below (in black-red): 6D images taken with a confocal microscope after red fluorescent staining of the bacterial biofilm. Left: high density of biofilm; Right: a significant decrease in the amount of biofilm following the addition of the substance ANKXNUMX.

Scientists at the Technion succeeded in damaging the defense mechanism of salmonella bacteria using substances originally developed against Alzheimer's disease

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The scientists demonstrated the new method on sulfur oxide molecules consisting of two oxygen atoms and one sulfur atom. These molecules have an axis determined by the oxygen atoms, and perpendicular to it is the sulfur atom. Courtesy of the Weizmann Institute

Molecular order exercises

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A new X-ray imaging method makes it possible to obtain XNUMXD videos of chemical reactions. Illustration: SLAC National Accelerator Laboratory.

The fastest films capture molecules in motion

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Cross section of the large subunit of the bacterial ribosome. In yellow - the exit tunnel of the proteins from the ribosome. In red - the binding pocket of erythromycin at the entrance to the tunnel. Bottom right (marked in light blue) – the ribosomal protein L22. In structural and chemical terms, the protein is distant from the binding pocket of the antibiotic. Source: Weizmann Institute magazine.

Researchers have discovered how a mutation in a ribosomal protein helps bacteria develop resistance to antibiotics

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Prof. John Sader, University of Melbourne

A revolutionary method for weighing a single molecule

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General structure of the skin layer together with melanocyte cells and a melanoma type cancer tumor. Photo: shutterstock.

First decoding of tyrosinase enzyme activity

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Using X-ray crystallography, researchers at St. Louis University have published the first ever image of the important blood clotting protein known as prothrombin (coagulation factor II). The flexible structure of the protein is a key component in the development of blood clotting. [Courtesy of Saint Louis University].

How does blood clot in the body?

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Dorothy Crawford-Hodgkin. From Wikipedia

Dorothy Croft Hodgkin - Queen of Africa and pioneer of X-ray crystallography

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The three-dimensional structure of the acetylcholinesterase enzyme molecule, with acetylcholine (center, in light green) within the active site

Good delay

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Right: CEO of L'Oreal Israel Nava Ravid, Dr. Gali Golan and Minister of Science Daniel Hershkowitz. Photography: Lem-Wlitz Studio

How can hyperase protein activity be controlled to prevent it from assisting in the production of blood vessels for cancer tissue?

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