PhD Studentship available in the Berntsson lab

There is one open position for a fully funded PhD studentship available in the Berntsson lab. For further info and to apply, please see:

Postdoctoral fellowships available in the Berntsson lab

The Berntsson lab at the department of Medical Biochemistry and Biophysics at Umeå University, Sweden, is looking to recruit up to two postdoctoral fellows (2-year fellowships, funded by the Kempe Foundation) to study the structural and functional aspects of Type 4 Secretion Systems. These large protein complexes are responsible for horizontal gene transfer between bacteria. As such, they facilitate the spread of, among other genes, antibiotic resistance between bacteria, both intra- and interspecies. 

The overall goals of these projects are to structurally and functionally characterize the DNA processing proteins of G+ Type 4 Secretion Systems. Parts of this project, for work on the T4SS from the pCF10 plasmid from Enterococcus faecalis, has already been started in the lab, but we are now also planning on expanding to other model systems. The projects will involve molecular biology, biochemistry and structural biology techniques, with an early emphasis on the functional characterization of these proteins and their complexes, followed by structural determination. 


The applicants must possess a PhD, or another diploma deemed equivalent to a PhD, within molecular biology, biochemistry, structural biology or a related field. Furthermore, the applicant must have practical experience and expertise of cloning and protein production and purification in bacteria. The applicant should preferably be experienced with functional studies of (membrane) proteins using various molecular biology and biochemical methods, such as ITC, SPR and fluorescence spectroscopy. Previous experience of working with gram-positive bacteria and membrane proteins is an advantage, as is previous experience of X-ray crystallography and electron microscopy. The applicants must have a very good level of English, both written and spoken. The applicants are also expected to be good team players, but should also be able to work independently. 


The application should consist of the following:

  1. A motivation letter (max 1 A4), where you highlight why you want to join the lab and study T4SSs. This letter must also include your contact information.
  2. The Curriculum Vitae of the applicant, including a list of published peer-reviewed articles.
  3. Copies of the PhD diploma (or equivalent).
  4. Contact details for three references, of which one should be your PhD supervisor.

The Berntsson lab is part of the Integrated Structural Biology community at Umeå University, consisting of 14 research groups that use, and have access to, high-field NMR, X-ray crystallography (including regular synchrotron access), world-class cryoEM and computation biology with a high performance computing centre.

The duration of the fellowship is 2 years. Your application should be written in English and prepared as a single package in PDF format, to be submitted to Make sure to use the subject line: “postdoc application 2019-04” in the application email. Submit the application on April 25, 2019 at the latest. The top ranked candidates will be contacted within three weeks from the closing date for an interview. Starting date according to agreement. For more information about the research or other details, do not hesitate to contact Ronnie Berntsson.

Email: ronnie.berntsson@umu.seWebpage:

New Article in Cell Reports: Control of bacterial virulence through the peptide signature of the habitat

Krypotou, E., Scortti, M., Grundström, C., Oelker, M., Luisi, B.F., Sauer-Eriksson, A.E. & Vázquez-Boland, J. Control of bacterial virulence through the peptide signature of the habitat. (2019) Cell Reports, 26, 1815-1827.

We identify a major control mechanism of Listeria virulence based on antagonistic regulation by environmental peptides.Activity levels of the virulence regulator PrfA depend on the net balance between the rates of synthesis of the PrfA-activating cofactor GSH from exogenous peptide-derived cysteine and of direct, promiscuous PrfA inhibition by non-cysteine-containing peptides

New ISB Article by Erik Johansson et al in Nature Communications

Professor Erik Johansson has published an article in Nature Communications named “Structural consequence of the most frequently recurring cancer-associated substitution in DNA polymerase epsilon“. The study was a collaboration with Uppsala University and University of Nebraska Medical Center. The article can be found at: “”

Magnus Wolf-Watz named professor

Magnus Wolf-Watz was named professor in biophysical chemistry on May 1:st 2018.

Ronnie Berntsson awarded the Swedish Foundation Starting Grant

Ronnie Berntsson has be awarded the Swedish Foundation Starting grant for research on Type 4 Secretion Systems.

For more info see:


Collaborative grant for flavivirus research

The Swedish Research Council has decided to award a 25.2 MSEK grant to a coalition of research groups at Umeå University and the University of Helsinki within the call “Research environment grant within infection and antibiotics”.

The project “Multimodal imaging and proteomics to study flavivirus replication and molecular disease mechanisms” is headed by flavivirologist Anna Överby Wernstedt at Umeå University and includes the biostruct-affiliated group of Lars-Anders Carlson. The other two teams involved in the collaboration are the Umeå-based group of Richard Lundmark and the Helsinki-based group of Sarah Butcher.

Ronnie Berntsson is as of now a Wallenberg Molecular Medicine Fellow

As of 1st of December Ronnie Berntsson has started as a Wallenberg Molecular Medicine Fellow at Umeå University.

New Integrated Structural Biology article: “Formation of a translocation competent protein complex by a dynamic wrap-around binding mechanism.”

This paper from the Wolf-Watz lab describes the discovery of a fundamentally new mechanism underlying protein-protein interactions. The chaperone-binding domain of the Yersinia effector protein YopH was found to lose its globular structure upon formation of a wrap-around architecture with its chaperone SycH. The mechanism is best described as a coupled binding and disordering event. The finding was enabled by an integrated structural biology approach by a five-lab effort and centered on NMR, SAXS and computational chemistry.

The article is published in Journal of Molecular Biology (2018), 430, 3157.