Welcome to the 1st BioStruct MasterClass 2010 "Approaches to determine Protein Structures"

The NRW Research School BioStruct is an international graduate school at the Heinrich-Heine-University in Düsseldorf with a focus on structural biology and their application in molecular medicine and biotechnology. International fellows do research here in 21 working groups from the Faculty of Mathematics and Natural Sciences, Medical Faculty, the Research Center Jülich and the Max-Planck-Institute for Bioinorganic Chemistry in Mülheim.

BioStruct’s MasterClass 2010 is organized by the PhD-Fellows of NRW Research School BioStruct. This meeting will bring together students from diverse backgrounds with renowned scientists in the area of structural biology research.

Therefore the NRW Research School BioStruct invites young researchers from the field of Structural Biology to the 1st ‘BioStruct’s MasterClass 2010’, at


Heinrich Heine Universität, Düsseldorf

September 06-09, 2010

Building 26.11.00, lecture hall 6C


We have invited speakers to provide us a deep insight into complex structural biology techniques. We also invite students to give 15 minute oral presentation or poster presentation based on their research work.

During the Master Class 2010 there will be time for networking in addition to scientific presentations, discussions and poster presentations. For example, a visit to the famous old town of the state capital Düsseldorf and a barbecue in a relaxed atmosphere on the campus of the Heinrich-Heine-University are planned.

We look forward to welcome you at the MasterClass and are available for any questions you may have. More information can be found at www.biostruct.de.


Monday, September 6th, 2010

11:00 Registration at the lecture hall 6B, building 26.11.O0
12:30 Welcome by Michael Piper, Rector of the Heinrich-Heine University Düsseldorf Welcome by Prof. Detlev Riesner Welcome by Lutz Schmitt, Chairman of BioStruct
13:15 - 15:00 Bernadette Byrne, ‘Production of membrane proteins for structural and functional studies’
15:00 - 15:30 Tea/Coffee break
15:30 - 15:50 Simon Sindbert, ‘Single molecule FRET accurately measures structure, dynamics and heterogeneities of an RNA four-way junction‘
15:55 - 16:15 Jonathan Mueller, ‘A heterodimer of human 3 -phospho-adenosine-5 -phosphosulphate (PAPS) synthases is a new sulphate activating complex‘
16:15 - 16:30 Tea/Coffee break
16:30 - 18:15 Ben Schuler, ‘Structure and dynamics in protein folding from single molecule fluorescence spectroscopy’

Tuesday, September 7th, 2010

09:00 - 10:45 Eckhard Hofmann, ‘Introduction into X-ray crystallography’
10:45 - 11:15 Tea/Coffee break
11:15 - 11:35 Badri Nath Dubey, ‘Insights into structure-function relationships in GTPase- effector interaction: a progress report‘
11:35 - 11:55 Chunmao He, ‘Structural features required for the protein-based sensing of nitric oxide - Insight from the spectroscopic investigations of ferrous nitrophorins‘
11:55 - 12:15 Arpita Roychoudhury, ‘Stabilization of membrane proteins using compatible solutes
12:15 - 13:00 Lunch
13:00 - 14:00 Poster session (odd numbers)
14:00 - 15:45 Helmut Grubmüller, ‘Biomolecular nanomachines at work: Computer simulation of conformational dynamics and single molecule experiments ’
15:45 - 16:15 Tea/Coffee break
16:15 - 18:00 Daniel Müller, ‘AFM: A nanotool complementing structural biology of biological membranes’
19:00 Congress Dinner at Restaurant "Brauerei Schiffchen"

Wednesday, September 8th, 2010

09:00 - 10:45 Michael Sattler, ‘Biomolecular NMR-spectroscopy for structural analysis of protein complexes in solution’
10:45 - 11:15 Tea/Coffee break
11:15 - 11:35 Hoa Quynh Do, ‘Mobility and topology of VPU and CD4 proteins by solid state NMR spectroscopy‘
11:40 - 12:00 Sven Schünke, ‘Structural insights into conformational changes of a cyclic nucleotide-activated ion channel binding domain in solution‘
12:00 - 13:00 Lunch
13:00 - 14:00 Poster session (even numbers)
14:00 - 15:45 Eckhard Bill, ‘Radicals coordinated to transition metal ions - Where are the electrons ? (EPR and Mössbauer Spectroscopy)’
15:45 - 16:15 Tea/Coffee break
16:15 - 18:00 Andrew Leslie, ‘Challenges in structural molecular biology’
19:00 BBQ at the Botanical Garden

Thursday, September 9th, 2010

09:00 - 10:45 Holger Stark, ‘Studying structure dynamics of large macromolecules by cryo-EM’
10:45 - 11:15 Tea/Coffee break
11:15 - 11:35 Harish Thakur, ‘Purification and characterization of the centrosomal protein TACC3‘
11:40 - 12:00 Justin Lecher, ‘Structural characterisation of the C39 peptidase like domain of ABC-transporter HlyB‘
12:00 - 13:00 Lunch
13:00 - 14:45 Clemens Glaubitz, ‘Biophysical studies on membrane proteins by solid-state NMR’
14:45 - 15:15 Best Poster Award and Closure by Dieter Willbold, Chairman of BioStruct


Eckhard Bill is group leader at the Max Planck Institute for Bioinorganic Chemistry in Mülheim an der Ruhr. In his laboratory for ‘Molecular Paramagnetism and Bioinorganic Spectroscopy’ they combine 57Fe-Mössbauer spectroscopy, multi-frequency electron-paramagnetic-resonance spectroscopy (EPR), static magnetic susceptibility measurements, and magnetic circular-dichroism spectroscopy (MCD) for the study of bioinorganic compounds and metalloproteins. Low temperature measurements and magnetic fields (flux up to 7 and 10 Tesla) are regularly applied for the investigation of complex systems.

Bernadette Byrne is an expert in the production of membrane proteins for structural studies. Successes have included production, crystallisation and ultimately structure determination of the important respiratory enzymes: formate dehydrogenase-N and nitrate reductase-N from E. coli. More recent work in her group has focussed on the production of challenging membrane proteins including human G-protein coupled receptors and bacterial transporters. The inherent hydrophobic properties of these proteins has necessitated the development of novel methodologies, to deal with the key problem of non-specific aggregation of membrane protein at high concentrations.

Clemens Glaubitz is Professor at the Institute of Biophysical Chemistry and Managing Director of the Centre of Biomolecular Magnetic Resonance at the Goethe University in Frankfurt. Solid-state NMR spectroscopy is at the heart of the research projects of his group. They analyze the structure-function relationship of multidrug transport proteins directly within the lipid bilayer, investigate Proteorhodopsin in marine bacteria, look for structure and function of G protein-coupled receptors (GPCRs) and are interested in the mechanism by which GPCRs transfer information across the membrane.

Helmut Grubmüller is the managing director of the Max Planck Institute for Biophysical Chemistry in Göttingen, director of the Department of Theoretical and Computational Biophysics and Professor for Physics at the University of Göttingen. The theoretical biophysics group aims to contribute to the understanding of the physics and function of biomolecules - particularly proteins - at the atomic level. They wonder how a given protein work and how these structural and dynamical properties can be described in terms of many-body systems. New statistical mechanics concepts, quantum hybrid methods, and efficient parallel simulation algorithms and codes are the methodological focus of the department.

Eckhard Hofmann is head of the protein crystallography situated in the department of biophysics. The group is an integral part of the Protein Research Department at the Ruhr-University Bochum. To generate an atomic model of proteins and to generate a 3D- structure the group uses the method of X-ray protein crystallography. One focus of their work lies on proteins from the photosynthesis apparatus of algae and bacteria. Another area of interest is membrane proteins involved in active transport across the cytoplasmic membrane.

Andrew Leslie is group leader in the Division ‘Structural Studies’ at the MRC Laboratory of Molecular Biology in Cambridge, UK. He works on projects to determine the atomic structures of macromolecular complexes and membrane proteins using X-ray diffraction. His group aims to determine the structure of ATP synthase from mitochondria and is also working on integral membrane proteins, a wide variety of which perform crucial activities in living cells.

Daniel Müller holds the Chair of Biophysics at the ETH Zürich, Department of Biosystems Science and Engineering (D-BSSE). His research group develops bionanotechnological methods that allow high-resolution imaging (~ 1 nm) and quantifying inter- and intramolecular interactions of biological processes. Currently these methods allow to image proteins at work at (sub-)nanometer resolution, to quantify and localize cellular interactions at molecular resolution and to observe how individual receptors of living cells communicate.

Michael Sattler is Director of the Institute of Structural Biology at the Helmholtz Zentrum München, Neuherberg and Professor for Biomolecular NMR-Spectroscopy at the TU München. A main focus in the Sattler group is to understand the structural basis of protein-protein and protein-RNA interactions that are functionally important for various aspects of gene expression, such as the regulation of (alternative) pre-mRNA splicing and gene silencing by non-coding RNAs (siRNAs, miRNAs).

Ben Schuler is Professor for Biochemistry at the Biochemical Institute of the University Zürich. In his research projects he investigates the folding, misfolding, and dynamics of proteins in a multidisciplinary approach, using a close combination of biochemical and biophysical methods, in particular single molecule fluorescence spectroscopy. Especially in combination with Förster resonance energy transfer (FRET), the intrinsically heterogeneous processes of both folding and misfolding of proteins are tested by quantifying structural distributions, their dynamics, and the underlying molecular mechanisms.

Holger Stark is leader of the BioFuture group at the Max-Planck-Institute for Biophysical Chemistry in Göttingen. The work in his group is focused on 3D structure determination of large macromolecular complexes by single particle electron cryomicroscopy (cryo-EM). The major research interest concentrates on macromolecular complexes related to pre-mRNA splicing, translation and cell cycle regulation and on the development of new methods to improve sample preparation, imaging and computational image processing techniques.

Responsible for the content: E-MailBioStruct Office