Structural Biology

Structural Biology comprises studies of proteins and nucleic acids, how they interact and how they appear in solution. The answer provides insight in to the function of the macromolecules and can explain diseases, basic functions or be used to understand mechanisms and in the longer perspective aim in drug design to name a few of the important areas where the techniques contributes.

Important techniques for structural biology include Cryo-EM, Nuclear Magnetic Resonance and Structural Proteomics and all of these are available through SciLifeLab. For a structural biology project, there is a pipeline starting with the gene and the end goal information is how and where the encoded protein functions or interacts with the surround.

It has become clear over the years that no technique alone can provide a full insight into a biological problem. Thus an integrated approach where different techniques are combined is often necessary. The aim for us working with structural biology at SciLifeLab is to be a partner along the whole way, from gene to final answer.

Structural biology techniques not available within SciLifeLab are part of our network, as important stake holders, and we will help you get in contact with the most appropriate partner. Users can reach many infrastructures important for structural biology from this single access point, at the SciLifeLab web.  

If you are interested to know more about one of our unit spanning projects, please read about BeyondFold.

SciLifeLab support within Structural Biology

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

Bioinformatics platform, National Bioinformatics Infrastructure Sweden (NBIS)

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 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 national resources in Structural Biology

ESS (The European Spallation Source)

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. 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.

Contact: Esko Oskanen

MaxIV Laboratory

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-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. 

Contact: Magnus Larsson

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


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. 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.

Contact: Dean Derbyshire

Contact us

Reach the team coordinating the SciLifeLab Integrated Structural Biology on:

Last updated: 2023-05-02

Content Responsible: David Gotthold(