CSSB: Newsletter 17

Kay Grünewald appointed new Scientific Director of CSSB

The Centre for Structural Systems Biology (CSSB) will be under new scientific management in 2022. Group leader Prof. Dr. Kay Grünewald from the Leibniz Institute for Experimental Virology (HPI) and the Department of Chemistry at the Universität Hamburg will be the new CSSB Scientific Director. On, 3 December 2021, the CSSB Council confirmed the CSSB Directorates election of Prof. Grünewald for a two-year term.

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Black Box Science: Part 4

The 4th episode of Rainer Kaufmann's video blog Black Box Science is now online. The episode is called "Covid and everyday scientific life."

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CSSB Seminar: JAN 14

On Friday, 14 January at 11:30, Dr. Pietro Scaturro from the Leibniz Institute for Experimental Virology (HPI) will give the first CSSB Seminar of 2022. All are welcome to attend!

Observing the secret life of molecules inside the cell

CSSB's Kosinski Group (EMBL) and colleagues have reconstructed the movements of the nuclear pore complex in living cells. The scientists were able to do this with the help of new software called Assembline, recently released by the Kosinski Group.

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New molecular insights into a rare neurological disorder

Investigations by the Sondermann group into the molecular mechanisms of the dynamin-related protein Atlastin (ATL) have revealed important insights that expand our understanding of a group of neurogenerative disorders.

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Wrangling an octopus-like viral replication machine

Researchers from CSSB's Grünewald group (HPI/ UHH) in collaboration with research groups from the Bernhard Nocht Institute for Tropical Medicine (BNITM) and EMBL Grenoble have studied nine structures of an essential Lassa virus protein in different functional states. The protein is necessary for virus replication and thus provides excellent targets for antiviral agents.

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Key Virulence Factor of Salmonella Characterized

Researchers from the Kolbe group in collaboration with researchers at CSSB's newest partner institution, Research Center Borstel FZB, as well as Max Plank Institute for Infection Biology, the University of Marburg and the Technical University of Braunschweig have revealed that FliB catalyzes a methyl transfer reaction which is mediated by an iron-sulfur cluster, [4Fe-4S].

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Structure of a promiscuous protein will help scientists design better drugs

Scientists from CSSB's Löw and Marlovits groups have determined the molecular structure of a gut protein that helps us absorb many drugs. This could help to develop drugs that reach target tissues more efficiently.

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