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Structural biology

fight against corona virus Illustration: Image by Fernando Zhiminaicela from Pixabay

Identifying a trap and finding the ultimate anti-coronavirus

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When disordered segments of protein molecules were first discovered in the late 80s, scientists used to cut them out and throw them away. Illustration: Dr. Hagen Hoffman's laboratory, Weizmann Institute

Not arranged and not by chance

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Hasilon's eyes - watching the bottom of the sea even in the dark. Photo: shutterstock

in the eye of the chasilon

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The active part of the molecule "Erncept" (threads in the colors of the rainbow) binds to the receptor of the Machupu virus (in gray). honey trap

A molecule that effectively neutralizes deadly viruses that pass from animals to humans

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Helix-shaped cholesterol crystals. Digital processing of data obtained from four different crystals in different cells using soft x-ray imaging under cold conditions (cryo-SXT)

The bad crystal

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the binding site. The researchers took a segment from the virus, which is known to be involved in the recognition of the receptor (marked in the colors of the rainbow), while it is bound to the corresponding segment in the receptor (marked in gray), and created crystals from them for examination using X-ray crystallography. The purple ball - the calcium ion that helped the binding process

A unique infection mechanism has been discovered, which a deadly virus uses to locate the target cells in the body and bind to them

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Breast cancer cells in culture as seen under an optical microscope. You can see the bands connecting the cells. Photo: Prof. Geiger, Weizmann Institute

All together and each separately

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Cells. Illustration: shutterstock

The genetic internet

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The fibers look like Legos in an electron microscope. Source: Weizmann Institute magazine.

Self-assembling proteins

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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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2D model of the human protein 2LANCL (in green) which is not known to bind metals. In yellow - the amino acids from which, according to the algorithm, the binding site is composed. The template according to which the model of the XNUMXLANCL protein was built contains a zinc ion whose position is marked in blue

Following the metal

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ribosome. Great protein. Illustration: shutterstock

See transparent

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The sapphire of the sea. Illustration: German nature artist Ernst Heckel, (1834-1919). From Wikipedia

How did the sea sapphire disappear?

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Scanning electron microscope photograph: A vesicle containing calcium carbonate nanoparticles, 20 to 30 nanometers in size, in a frozen sea urchin embryo sample

Actually - or what is the connection between the construction of the internal skeleton in mammals and corals with an external skeleton?

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A new method for XNUMXD printing was developed by Jennifer Lewis and her team at Harvard, using multiple print heads and an adapted 'ink' to create complex living structures, along with the tiny blood vessels. Click here to see how it works. Photo: Wise Institute at Harvard University and SEAS

An important step towards XNUMXD printing of living tissues

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Prof. Yoel Sussman. Photo: Weizmann Institute

Insects will serve as "factories" for human proteins

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Prof. Yoel Sussman and Prof. Israel Silman. excessive speed. Photo: Weizmann Institute

The Instruct Center at the Weizmann Institute was selected as one of seven European core centers in structural biology

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