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.
Hamburg, 6 July 2017 CSSB opens its doors On 29 June, at a ceremony in front of 700 guests, the Centre for Structural Systems Biology (CSSB) in Hamburg, was officially opened. At the event on the Deutsches Elektronen-Synchrotron (DESY) Campus in Hamburg, Helmut Dosch, Chairman of the DESY Board of Directors, presented Head of EMBL Hamburg and CSSB Scientific Director Matthias Wilmanns with a key to the building in front of the assembled guests.
Hamburg, Vienna and Amsterdam, 11 April 2017 Structure of key system for TB infection revealed In a paper published this week in Nature Microbiology, the Wilmanns group at EMBL together with scientists from across Europe reveal the overall architecture of an assembly of proteins known as Type VII secretion systems found in a group of bacteria which cause diseases such as tuberculosis.
Hamburg, 2 December 2016 Catching the chaperone in the act “I probably should have thrown those protein samples away,” says EMBL group leader Christian Löw. In 2009, one year into his postdoc, Löw was struggling to make any headway with his research into membrane proteins and set up yet another crystallisation trial in the vain hope of making that long awaited step forward. “I knew the prepared batch was contaminated with other proteins before we even started,” he says. “But we were under so much pressure to get results we went ahead anyway.” Predictably, the membrane protein he needed failed to crystallise. Yet Löw had unwittingly shone light on another group of proteins.
Hamburg, 31 August 2016 Taking crystallography to the fourth dimension “Now we have the right people, in the right place, with the right technology!” exclaims EMBL group leader Thomas Schneider, who coordinates activities at the EMBL crystallography beamlines on DESY’s light source PETRA III in Hamburg. Together with Arwen Pearson, Professor at the Centre for Ultrafast Imaging (CUI), Universität Hamburg, he and his team have been laying the groundwork to take crystallography – his structural biology method of choice – into a new time dimension.
Hamburg, 8 August 2016 Blocking the waste disposal unit Cancer cells are more dependent on a cellular garbage disposal unit – the proteasome – than healthy cells, and cancer therapies take advantage of this dependency. The Schneider group at EMBL Hamburg and colleagues at MPI Göttingen have now succeeded in determining the 3D structure of the human proteasome in unprecedented detail and have deciphered the exact mechanism by which inhibitor drugs block the proteasome. Their surprising results, published in Science, will pave the way to develop more effective treatments.