Alexey Amunts

Alexey Amunts


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Arbetar vid Institutionen för biokemi och biofysik
Telefon 08-16 10 03
Besöksadress Science for Life Laboratory, Tomtebodavägen 23, Box 1031, 171 65 Solna
Rum SciLifeLab y3
Postadress Institutionen för biokemi och biofysik 106 91 Stockholm


Electron cryo-microscopy visualisation of macromolecules.

The most definitive way to understand molecular mechanisms of a living cell is to directly visualize its components by obtaining their 3D structures. Beyond basic science, structural information on molecules is essential for drug design and optimization of therapeutic compounds. Recent advances in Electron Cryo-Microscopy (cryo-EM) have made it now possible to determine otherwise intractable macro-molecular complexes including membrane proteins at near atomic resolution.

Our group at Science for Life Laboratory in Stockholm further explores the frontiers of the cryo-EM methodology to visualize macromolecules that play key roles in fundamental and medically relevant cellular processes. The lab benefits from the state-of-the-art cryo-EM equipment, including Titan Krios and Talos Arctica armed with the latest generation direct electron detectors, modern computational infrastructure and skilled microscopists.

We are interested in complex questions and technically challenging subjects, for which the molecular mechanisms and dynamics have been least understood. One of the ongoing projects is to characterize the entire mechanism of protein synthesis in mitochondria. We also focus on membrane proteins and bioenergetics related complexes, where intrinsic flexibility and dynamic properties underlie functional characteristics. To realize these proposals, we use a combination of genetic and biochemical methods, while simultaneously developing new methods for direct visualization of molecules in its close to native environment.



Course: Structural Biochemitry, 15 ECTS. 

Content: 65 hours of frontal lectures, 18 hours of computational exercise, 16 hours of lab practice (X-tay crystallography and NMR), 14 hours of cryo-EM practice.

Level: given annualy to 25 advanced undergraduate and Master students.

Term: August to October


Group members

Juni Andréll, Researcher

Karin Walldén, Researcher

Shintaro Aibara, Postdoc

Yuzuru Itoh, Postdoc

Narges Mortezaei, Postdoc

Alexander Mühleip, Postdoc

Laura Orellana, Postdoc

Annemarie Perez Boerema, PhD Student

Victor Tobiasson, PhD Student

Hermina Wieske, Master Student

Shalini Sinha, Research Assistant


Work Opportunities

We offer PhD and Postdoc positions as well as short training projects for highly motivated researchers. The lab provides stimulating and collegial environment for people who want to study something important, develop themselves further, work hard and aim high.

– You will be tackling a difficult subject, you are genuinely interested in and enjoying working on.

– You will be offered ample resources, long-term support and collaborations.

– You will be expected to show determination, be proactive, creative and preferably nice to your colleagues.                                      

Please contact  Alexey Amunts


Structural Biology discussion group

We gather a weekly discussion group at SciLifeLab to better understand the current practice of cryo-EM, present the most recent developments and applications to interesting biological problems. The list of upcoming speakers is found here 

We encourage everyone to take active part.


Visiting address

Science for Life Laboratory, Tomtebodavägen 23A, 17165 Solna, Sweden



I urval från Stockholms universitets publikationsdatabas
  • 2017. Nirupa Desai (et al.). Science 355 (6324), 528-531

    Mitochondria have specialized ribosomes (mitoribosomes) dedicated to the expression of the genetic information encoded by their genomes. Here, using electron cryomicroscopy, we have determined the structure of the 75-component yeast mitoribosome to an overall resolution of 3.3 angstroms. The mitoribosomal small subunit has been built de novo and includes 15S ribosomal RNA (rRNA) and 34 proteins, including 14 without homologs in the evolutionarily related bacterial ribosome. Yeast-specific rRNA and protein elements, including the acquisition of a putatively active enzyme, give the mitoribosome a distinct architecture compared to the mammalian mitoribosome. At an expanded messenger RNA channel exit, there is a binding platform for translational activators that regulate translation in yeast but not mammalian mitochondria. The structure provides insights into the evolution and species-specific specialization of mitochondrial translation.

  • 2016. Martin Ott, Alexey Amunts, Alan Brown. Annual Review of Biochemistry 85, 77-101

    Mitochondria are essential organelles of endosymbiotic origin that are responsible for oxidative phosphorylation within eukaryotic cells. Independent evolution between species has generated mitochondrial genomes that are extremely diverse, with the composition of the vestigial genome determining their translational requirements. Typically, translation within mitochondria is restricted to a few key subunits of the oxidative phosphorylation complexes that are synthesized by dedicated ribosomes (mitoribosomes). The dramatically rearranged mitochondrial genomes, the limited set of transcripts, and the need for the synthesized proteins to coassemble with nuclear-encoded subunits have had substantial consequences for the translation machinery. Recent high-resolution cryo-electron microscopy has revealed the effect of coevolution on the mitoribosome with the mitochondrial genome. In this review, we place the new structural information in the context of the molecular mechanisms of mitochondrial translation and focus on the novel ways protein synthesis is organized and regulated in mitochondria.

Visa alla publikationer av Alexey Amunts vid Stockholms universitet


Senast uppdaterad: 15 oktober 2017

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