Hamburg, 6 December 2019 Understanding a key player in melanoma A new paper describes the mechanism that the transcription factor MITF, a key member of the MIT/TFE family, uses for selecting its partners. It is the result of a collaboration between the groups of Matthias Wilmanns, Head of EMBL Hamburg, and Eiríkur Steingrímsson from the University of Iceland, Reykjavík, and new chair of the EMBL Council. MITF plays a key role in the development of Melanoma. Understanding its function could be key for treating this disease.
Hamburg, 18 July 2019 First results from CSSB Six research groups, among them the García Alai team and the Löw group from EMBL Hamburg, have developed a protocol that will simplify the process of solubilising integral membrane proteins (IMPs), as they report on 17 July in Scientific Reports. This is also the first publication resulting from a collaboration at the Centre for Structural Systems Biology (CSSB) in Hamburg.
Hamburg, 17 June 2019 EMBL and Tara: Hamburg Mission Microplastics, the Tara Ocean Foundation’s expedition studying the microplastics entering European waters, recently brought the schooner Tara to the German city of Hamburg and the estuary of the river Elbe. Here, head of EMBL's Hamburg Unit, Matthias Wilmanns, discusses plastic pollution and infectious disease research at EMBL.
Hamburg, 18 February 2019 Cell death trigger in tuberculosis bacteria Tuberculosis (TB) is one of the top ten causes of death worldwide. The genome of the bacterium that causes TB holds a special toxin-antitoxin system with spectacular action: once the toxin is activated, all bacterial cells die, stopping the disease. A research team co-led by the Wilmanns group at EMBL in Hamburg investigated this promising feature for therapeutic targets, and now shares the first high-resolution details of the system in Molecular Cell.
Hamburg, 4 February 2019 Structure of prodrug-transporter complex revealed Research groups lead by CSSB/EMBL scientists Christian Löw and Jan Kosinski are now a step closer to understanding the structures of peptide transporters and how they recognise, bind and transport prodrugs. The groups recently determined a high-resolution crystal structure of a peptide transporter in complex with the prodrug valganciclovir: a medication that combats certain viral infections. Their results, published in the Journal of the American Chemical Society, could assist in the design of prodrugs with improved absorption rates.
Hamburg, Heidelberg, 7 November 2018 New insights into the regulation of haemostasis EMBL researchers in Hamburg and Heidelberg and their collaborators have studied a key protein involved in haemostasis, known as the von Willebrand factor (VWF). In a paper published in Blood, they report the structure of a key region of VWF known as the C4 domain. In a second paper, also published in Blood, a group from the University Medical Center Hamburg-Eppendorf (UKE) in collaboration with the Hamburg group reports on a clinically relevant mutation in the C4 domain. Matthias Wilmanns, group leader at EMBL Hamburg, and Janosch Hennig, group leader at EMBL Heidelberg, teamed up for a collaboration between two EMBL units with a focus on structural biology.
Hamburg, 31 October 2018 Time-resolved X-ray crystallography simplified An international collaboration has developed a new method to observe the molecular foundations of biology, with the help of beamline P14 at EMBL Hamburg. The new ‘hit-and-return’ method simplifies and accelerates time-resolved X-ray crystallography experiments, allowing many snapshots to be recorded in a single experimental session.
Hamburg, 22 October 2018 ARP/wARP 8.0 released Researchers in the Lamzin group at EMBL Hamburg have released the next generation of their ARP/wARP software. ARP/wARP is used by structural biologists, enabling them to automatically build models of proteins and their complexes, including nucleic acids and small molecule ligands, based on crystallography data collected using synchrotron beamlines. This latest version is also able to interpret cryo-EM density maps at a resolution of 3.5 Å and to construct some partial models even at 4.5 Å resolution.
Hamburg, 13 September 2018 X-rays reveal surprising shape of scaffolding protein While bioinformatics tools had suggested that the four domains of PDZK1 would behave like beads on a string, moving around in a highly flexible manner, X-ray experiments now show that PDZK1 actually has a relatively well-defined L-shaped conformation with only moderate flexibility. This discovery was led by EMBL Hamburg group leaders Dmitri Svergun and Christian Löw. The journal Structure publishes their results on 13 September 2018.