Integrated Structural Biology
The new ISB platform includes The Swedish NMR Centre and the Structural Proteomics Units and is virtually linked to the SciLifeLab CryoEM unit. The platform coordinates the service area together with stakeholders such as MAX IV, ESS, PPS and ProLinC. This means that users will soon be able to reach all structural biology technologies from a single access point at the SciLifeLab web. Together with the InfraLife project and SciLifeLab offices in Linköping, Lund, Gothenburg and Umeå, the ISB platform extends the national scope of SciLifeLab.
Any questions – Cecilia’s your guy!
Core Facility
Structural Proteomics
ESS
MaxIV
ProLinc
Protein Production Sweden
Nuclear Magnetic Resonance
Nuclear Magnetic Resonance
Cryo EM
InfraLife
National Bioinformatics Infrastructure Sweden
Call for an Expression of Interest to host DDLS Data area nodes and WABI
The Data-Driven Life Science (DDLS) program coordinated by SciLifeLab and funded by the Knut and Alice Wallenberg Foundation releases a new Expression of Interest (EoI) call for the 11 partners institutions.
SciLifeLab Infrastructures
Nuclear Magnetic Resonance
NMR is a spectroscopic method that will provide insight at the atomic level. Signals are representing individual atoms and therefore one can use each atom in the molecule as a reporter, gaining insight into dynamics as well as specific interactions. NMR is also a method that can be used for structure determination, and is a good choice when Cryo-EM or crystallography is not feasible.
Contact: Cecilia Persson
Cryo EM
Cryo-Electron Microscopy is a technique for visualizing macromolecular structures using a transmission electron microscope which permits samples to be studied at cryogenic temperatures. Cryo-EM does not require large sample sizes or crystallization and is therefore suited to the visualization of structures at near-atomic resolution. Moreover, structures can be flash-frozen in several conformations to allow biological mechanisms to be deduced. In recent years, there has been a significant increase in the achieved resolution (the Cryo-EM revolution) mainly due to the development of direct electron detectors and the improvement of image-processing algorithms.
Contact: Jose Miguel de la Rosa Trevin
InfraLife
The InfraLife initiative aims at connecting SciLifeLab, ESS and MAX IV infrastructures. By learning from each other and increasing knowledge about different research possibilities, InfraLife aim to make these large scale infrastructures more accessible for a wider user base including industry and healthcare. One of the first large projects is the “InfraLife Integrative Structural Biology course” running for two weeks on site starting in late August 2022.
Contact: Josefin Lundgren-Gawell
National Bioinformatics Infrastructure Sweden
NBIS at SciLifeLab is a distributed national research infrastructure providing bioinformatics support to the Swedish life science researchers community. Scientists across Sweden can contact NBIS for help on any bioinformatics-related questions, including protein structure modeling (e.g. with AlphaFold, Rosetta), receptor-ligand docking, and the best ways of integrating experimental information with protein models.
Contact: Claudio Mirabello
Structural Proteomics
The Structural Proteomics infrastructure unit provides access to cutting-edge equipment and expertise, for analysis of protein interactions and conformational dynamics with mass spectrometry. We provide service for all aspects of structural proteomics, including project planning, sample preparation, data collection and data analysis. Current Hydrogen Deuterium Exchange (HDX-MS) and Crosslinking Mass Spectrometry (XL-MS) services and workflows are well established and available to all users;
HDX-MS and XL-MS have different abilities and limitations. HDX-MS works in solution with only a few (up to three) purified components, can detect dynamic changes in structure and interaction interfaces, and is complementary to several other structural biology techniques, such as crystallography and cryoEM. XL-MS can be done on more complex samples, ranging from intact cells in culture to purified proteins in solution, and gives distance constraints between two peptides, which can be used in modeling or to complement data from NMR, crystallography or cryoEM. Even though both HDX-MS and XL-MS work on the peptide level, the resolution of HDX-MS is higher, and can at its best pinpoint events on the individual amino acid level
Contact: Simon Ekström
Other Infrastructures
ESS
The European Spallation Source ESS ERIC is a European project to build the world’s most powerful neutron source in Lund and is expected to open for first users in 2027. Neutron scattering can be used to investigate structure and dynamics in multiple time and length scales, ranging from the atomic to full organisms. Neutron scattering can provide unique information on e.g. hydoigen positions, composition of macromolecular complexes or membrane structure. Dedicated instruments will be available for the different neutron scattering techniques relevant for biology experiments, as well as supporting laboratory facilities for sample preparation and conditioning. Data processing and analysis support will be provided by the ESS Data Management and Software Centre in Copenhagen.
Contact: Esko Oskanen
MaxIV
The synchrotron light source MAX IV in Lund provides scientists with the most brilliant X-rays for research. Approximately 1500 national and international researchers from both industry and academia use the Swedish-based laboratory annually to conduct groundbreaking experiments in materials and life sciences.
The X-ray light is used for research at several experiment stations called beamlines. The beamlines can all be operated simultaneously and around the clock. At present 16 financed beamlines are either in operation or under construction at MAX IV. In total, the facility is able to accommodate 26‒28 beamlines.
X-rays are one of the most important experimental tools in medicine, biology and the material sciences. The X-rays generated at MAX IV enable researchers to study details ranging from a few tenths of a nanometre to micrometers in size. It is done using various techniques including imaging, spectroscopy, diffraction and scattering methods. Techniques are often combined and can provide completely new knowledge about biological samples and processes with unprecedented resolution in both space and time.
Some examples of the use of synchrotron radiation in the life sciences is the development of new active compounds or delivery systems for drugs or to study healthy and diseased cells and tissue as a basis for developing new medical treatments but many other applications are possible in biotechnology, food and environmental science, medtech and other relevant fields.
Contact: Selma Maric
Protein Production Sweden
For many structural biology experiments, access to excellent protein reagents of high purity is a prerequisite. PPS is a national research infrastructure with dedicated expertise to help you with producing recombinant proteins for your research needs. To cover most types of proteins, we work with several cellular expression systems for protein production and various purification techniques. PPS can also perform specific labelling of proteins when needed.
Contact: Malin Bäckström
ProLinc
Understanding the biological function of proteins, their interactions, and activities within expanded pathways, requires at some point for practical purposes the necessity to analyse protein structures. Structural biology techniques are plagued with complications arising from sample quality.
Indeed, as such most, if not all, methods for structure analysis have stringent requirements on sample quality and behaviour: if test subjects are flawed no methodology will generate meaningful results and will only serve to waste resources!
The ‘Protein folding and Ligand Interaction Core’ facility at Linköping university (ProLinC)houses a diverse range of complementary biophysical techniques for the assessment and characterization of proteins and their complexes. ProLinC is routinely utilised for sample assessment ahead of structural determination activities.
It should be noted that sample purity is not generally the most important property that impacts structural methods, although impurities can result in difficulties interpreting results from biophysical methods. Of course, said biophysical methods are crucially required for assessing sample behavior – such as [poly]dispersity, complex integrity, and effects of buffer formulation – which is critical to the success of structure analysis.
Contact: Dean Derbyshire
Contact us
Reach the team coordinating the ISB Platform on: isb@scilifelab.se