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.
Hamburg, 10 May 2016 Enzyme with a dual-purpose loop A closer look at the 3D molecular structure of Death Associated Protein Kinases (DAPK) reveals an unexpected dual-purpose loop in the folded string of amino acids. Work by researchers in the Wilmann’s group at EMBL Hamburg, published in Structure, suggests that the small loop is crucial for dimer formation and calmodulin binding. “What started as a small side project, unearthed a complex and important signaling pathway within this group of kinases,” says Matthias Wilmanns, “It goes to show, you can’t always plan science!”
Hamburg, 24 March 2016 Better tools for exploring TB protein structures Information about the 3D structure of Mtb proteins involved in the infection process of tuberculosis can provide crucial clues for designing new drugs. However, Mtb proteins are not easy subjects for structural biology studies, and as a result relatively few have been characterised in detail. The need for improved methodology is driving efforts by the Wilmanns’ group at EMBL in Hamburg, who have optimised methods for producing the proteins in the laboratory, and now hope to share this knowledge with other structural biologists.
Hamburg, 4 February 2016 How to make a protein happy Over the years, the scientists at the Sample Preparation and Characterisation Facility (SPC) at EMBL Hamburg have acquired untold expertise helping users to get the best results by optimising protein samples for structural biology experiments. Today, two new tools they developed to determine the ideal conditions for protein stability, purification and storage, are commercially available. Stephane Boivin, a staff scientist who initiated the project, tells us more about the RUBIC Buffer and Additive Screens, and the journey from idea to commercial product.
Hamburg, 18 January 2016 The cellular crystal factory Scientists from the Wilmanns group have teamed up with experts from across the DESY research campus to show that naturally formed crystals can diffract X-rays. In a study published recently in the International Union of Crystallography Journal (IUCrJ), the team of Hamburg scientists successfully used crystals grown inside yeast cells for crystallography experiments at an X-ray free-electron laser facility at the SLAC National Accelerator Laboratory. "This could become a complementary method for structural biologists studying challenging proteins,” Wilmanns concludes.