12 Jan 2021

Cryo-EM data decode the mechanism behind the honeybee viral infections

How does the honeybee virus behave when infecting the host cell? Does it resemble pulling a note out of a bottle or rather opening a surprise egg? Karel Škubník and his colleagues, led by structural virologist Pavel Plevka from CEITEC Masaryk University, have discovered new findings describing the mechanism of genome release of honeybee viruses. They shed a new light on the exiting believe regarding behaviour of honeybee viruses during the host cell infection process. The scientists reached this remarkable conclusion with the help of cryo-electron microscopy combined with protein simulations, which were conducted by Robert Vácha and his research group. The research results were published on 1^st January 2021 in the international scientific journal Science Advances. More details are presented in the Research Highlight below.

11 Jan 2021

Instruct-ERIC Webinar Series: Structure Meets Function - Webinar #6

Featuring expert speakers from Instruct Centres across Europe, Instruct-ERIC Webinar Series: Structure Meets Function highlights some of the latest developments in structural biology, demonstrating how integrative methods are enabling scientists to decipher the mechanisms that underpin health and disease.

4 Jan 2021

New possibilities in fight against pathogenic bacteria – structure and role of protein HelD

Using cryogenic electron microscopy, three independent teams of researchers from Australia, the Czech Republic, and Germany have described the structure of a striking new complex between bacterial RNA polymerase and an accessory protein, HelD. The groups worked with a range of different components and organisms to gain a comprehensive understanding of how HelD uses a dramatic brute-force approach to prise open RNA polymerase and dislodge the tightly bound DNA and RNA.

This discovery provides an in-depth view of the bacterial transcription apparatus, and opens up pathways for development of urgently needed new antimicrobials capable of targeting serious pathogens such as the causative agent of tuberculosis. It leads to new possibilities of development of the much needed antimicrobials against serious pathogens, including the causative agent of tuberculosis. Their discoveries have been published in the Nature Communications Journal.

17 Dec 2020

Webinar series: What can iNEXT-Discovery do for us? Rebecca Thompson, ABSL, From protein sample to structure: getting started with single particle Som

The webinar series What can iNEXT-Discovery do for us? will continue on 21st December at 16:00 CEST with the topic From protein sample to structure: getting started with single particle Som presented by Rebecca Thompson, ABSL.

11 Dec 2020

New Protein Production facility at BIOCEV

The Centre of Molecular Structure at BIOCEV established a new Protein Production facility. This initiative follows the survey mapping a preliminary interest from potential users and resulted in a platform for both routine protein production and demanding development of methods in semi high-throughput format. The facility has been in a pilot mode since July 2020 to evaluate the feasibility for the long run. Now the new Protein Production facility has been added to CIISB application form and users can apply via the standard application process.

10 Dec 2020

Scientific presentations from Instruct-ULTRA General Assembly

The Horizon 2020 project Instruct-ULTRA aiming to accelerate the expanded implementation of Instruct by opening up to new members is nearing to its end. Scientific talks from the Instruct-ULTRA project's final General Assembly, held remotely in November 2020, are now available on-line as on-demand videos.

10 Dec 2020

Webinar series: What can iNEXT-Discovery do for us? Eva Pereiro, ALBA, A carthographic description of the cellular landscape by cryo soft X-ray tomography

The webinar series What can iNEXT-Discovery do for us? will continue on 14th December at 16:00 CEST with the topic A carthographic description of the cellular landscape by cryo soft X-ray tomography presented by Eva Pereiro, ALBA.

8 Dec 2020

AlphaFold: a solution to a 50-year-old grand challenge in biology

Proteins are essential to life, supporting practically all its functions. They are large complex molecules, made up of chains of amino acids, and what a protein does largely depends on its unique 3D structure. Figuring out what shapes proteins fold into is known as the “protein folding problem”, and has stood as a grand challenge in biology for the past 50 years. In a major scientific advance, the latest version of the AI system AlphaFold (deepmind.com) has been recognized as a solution to this grand challenge by the organizers of the biennial Critical Assessment of protein Structure Prediction (CASP). This breakthrough demonstrates the impact AI can have on scientific discovery and its potential to dramatically accelerate progress in some of the most fundamental fields that explain and shape our world.