Relion – Main Page

Below is link to a Main Page for RELION (for REgularised LIkelihood OptimisatioN, pronounce rely-on) from Sjors Scheres at the MRC Laboratory of Molecular Biology.

http://www2.mrc-lmb.cam.ac.uk/relion/index.php/Main_Page

relion21_tutorial

Grant’s EM course

A series of lectures by Grant Jensen at Caltech explaining cryo-EM technology to a great detail in a simple way:

http://cryo-em-course.caltech.edu/videos/  or  https://jensenlab.caltech.edu/courses/

NRAMM Workshop on Advanced Topics in EM Structure Determination

The talks from The National Resource for Automated Molecular Microscopy (NRAMM) Workshop on Advanced Topics in EM Structure Determination: Challenges and Opportunities (October 29 – November 3, 2017) are available on-line at: http://nramm.nysbc.org/2017-workshop-lectures/. Topics discussed  included specimen preparation, imaging, instrumentation, processing and reconstruction, and methods for validation. 

 

Nobel prize in chemistry awarded for method to visualize biomolecules

The Nobel prize in chemistry has been awarded to Jacques Dubochet, University of Lausanne, Switzerland, Joachim Frank, Columbia University, New York, USA, and Richard Henderson, MRC Laboratory of Molecular Biology, Cambridge, UK,

“for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution”

This is very exciting news and fantastic recognition for the whole Cryo-Microscopy Society! The Cryo-EM Unit at the University of Helsinki, headed by Prof Sarah Butcher, hosts state-of-the-art transmission electron microsope FEI Talos Arctica, which enables this technique in its full capacity. We are sure it will prove very useful for  future outstanding research in Finland.

https://www.nobelprize.org/nobel_prizes/chemistry/laureates/2017/press.html

Interview  in C& E News https://cen.acs.org/articles/95/web/2017/10/Cryo-electron-microscopy-innovators-win-2017-Nobel-Prize-in-Chemistry.html

Interview in Helsingin Sanomat https://www.hs.fi/tiede/art-2000005394534.html

Interview about all of the Nobel prizes in Helsingin Sanomat TV https://www.hs.fi/tiede/art-2000005401270.html

History of the high points of the field written by Peter Brzezinski of the Nobel Committee for Chemistry advanced-chemistryprize2017

 

One step forward in developing drugs against sepsis-causing virus in newborns

Resolving the high-resolution structure of a parechovirus by Prof Butcher’s group at the University of Helsinki helps the development of antiviral drugs.

Human parechovirus type 3 is a picornavirus that can cause severe infections in humans, resulting in sepsis and central nervous system disease in newborns. So far the most promising anti-picornaviral drug candidates do not have any effect on the parechovirus, therefore new effective means have to be found.

Researchers in the University of Helsinki have determined a high-resolution structure of the human parechovirus type 3. The three-dimensional model was created by collecting thousands of images of virus with an electron microscope under -190 °C. The images were then computationally aligned and combined.

“The virus genome is a single-stranded RNA, which is encapsidated in a protein shell. About a quarter of the genome is in close contact with the capsid proteins, leading to highly ordered RNA. This has not been seen in other picornaviruses,” describes Postdoctoral Researcher, Dr Shabih Shakeel in the Institute of Biotechnology.

The atomic model of the virus shows a distinct way of how viral proteins interact with each other to stabilize the capsid. The best studied anti-picornaviral drug pleconaril and its derivatives work well against enteroviruses, large group of picornaviruses. The parechovirus type 3 structure demonstrates that pleconaril binding place is blocked in parechoviruses and therefore does not work against this virus group.

Marie Curie Postdoctoral Research Fellow, Dr Ausra Domanska worked on the structure of the same virus in complex with antibody fragments recognising parechovirus type 3.

“In the absence of antiviral drugs, developing broadly neutralising monoclonal antibodies as therapeutic antibodies against this virus is one of the most promising treatment options for clinicians in the near future,” she says.

HPeV3-Fab15_ambient_23082016-croped

Human parechovirus type 3 with bound antibody fragments. Picture by Ausra Domanska

_________

Shakeel, S. et al. Multiple capsid-stabilizing interactions revealed in a high-resolution structure of an emerging picornavirus causing neonatal sepsis. Nat. Commun. 7:11387 doi: 10.1038/ncomms11387 (2016) http://www.nature.com/articles/ncomms11387

This study was supported by Academy of Finland, Sigrid Juselius Foundation, People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme FP7/2007-2013/ under REA grant agreements no. 612308 and no. 628150. The authors of the study, led by Prof. Sarah Butcher at the Institute of Biotechnology, University of Helsinki, and Dr Wolthers at Academic Medical Center in Amsterdam, are all members of the AIROPico consortium.

AIROPico (Academic Industry R&D Opportunities for Picornaviruses) is the first EU-funded scientific consortium for emerging picornavirus research. Coordinated by Dr Katja Wolthers from the Netherlands, AIROPico brings together researchers from two companies and four academic sites across Europe, and aims to shed new light on how picornaviruses cause disease in humans. The consortium’s objectives include the creation of fast point-of-care diagnostic tools and the development of effective anti-picornaviral treatment.

For more info about the AIROPico project see http://www.airopico.eu/

BI open day on 2nd October, 2015

Group members of Sarah Butcher’s lab presented their research to undergraduate students from University of Helsinki. The group created models of viruses at 2.8 million times magnification to demonstrate the structure of viruses and their interaction with cells.

BIOpenDay02102015

Post doc James Geraets at the poster actively discussing with a student