Czech Infrastructure for Integrative Structural Biology – CIISB
A gateway to realm of structural data for biochemists, biophysicists, molecular biologist, and all scientists whose research benefits from accurate structure determination of biological macromolecules, assemblies, and complex molecular machineries at atomic resolution.
Open access to 10 high-end core facilities and assisted expertise in NMR, X-ray crystallography and crystallization, cryo-electron microscopy and tomography, biophysical characterization of biomolecular interaction, nanobiotechnology, proteomics and structural mass spectrometry.
A distributed infrastructure constituted by Core Facilities of CEITEC (Central European Institute of Technology), located in Brno, and BIOCEV (Biotechnology and Biomedicine Centre), located in Vestec near Prague, Central Bohemia.
CEITEC Core Facilities
BIOCEV Core Facilities
Velké výzkumné infrastruktury - Operated by CESNET on behalf of the Council for Large Infrastructures for Research, Experimental Development and Innovation.
4th National Day of Large Research Infrastructures
The Ministry of Education, Youth and Sports of the Czech Republic and the Faculty of Mathematics and Physics of Charles University are honoured to invite you to take part in the 4th National Day of Large Research Infrastructures, to be held on 19th November 2019 in the premises of LINDAT/CLARIAH-CZlarge research infrastructure.
Instruct-ERIC International Access Call
We are delighted to announce the opening of the Instruct access call for International users.
Prof Wolfgang Baumeister awarded the 2019 Ivano Bertini Award for outstanding contributions to structural biology
The Ivano Bertini Award is offered by Instruct to recognise a significant achievement in frontier research that utilises an integrative structural biology approach.
The iNEXT workshop: Integrated methodologies and approaches for structural biology in Brno
jointly organized by CEITEC Masaryk University, University of Utrecht, Czech Infrastructure for Integrative Structural Biology, and Czech Society for Structural Biology, will provide a comprehensive overview of the state-of the-art progress of integrative methodologies to existing and potential users of iNEXT facilities. Nineteen prominent speakers will report on recent advances and developments in nuclear magnetic resonance (NMR), x-ray diffraction, small-angle x-ray scattering (SAXS), cryo electron microscopy and tomography (cryo-EM and cryo-ET), and computational structural biology. The workshop is open to all PhD students, postdoctoral fellows, and researchers at no cost. Registration is open till April 10, 2019.
Instruct Biennial Conference - Structural Biology: Deeper into the Cell
The 4th Instruct Biennial Structural Biology Conference will take place in Alcalá de Henares, Spain, from May 22 till May 24, 2019. The historical Alcalá de Henares was the original location of the Universidad Complutense, founded in 1293 and one of the oldest universities in the world, as well as being the birthplace of Miguel de Cervantes. The social programme of the meeting will include a visit to the city, a gala dinner and extensive opportunities to network with the Instruct Structural Biology community.
NAT. COMMUN. 2019
Summary showing CK1ε role in DVL3 conformational dynamics. A summarizing model which proposes at least three DVL conformations in vivo: (i) a closed (CK1ε present and inactive), (ii) open (CK1ε active), and (iii) non-physiological open, which occurs when CK1ε is absent or the DVL-CK1ε interaction is disrupted. Position of insertion of FlAsH III binding tag is indicated. The CK1-induced phosphorylation events are depicted as P in red circle and the C-terminus of DVL as red thick line. The molecular distance analysed in the FRET FlAsH sensor III is shown as a dashed red line; ECFP, enhanced cyan fluorescent protein
Dishevelled (DVL) is the key component of the Wnt signalling pathway. Currently, DVL conformational dynamics under native conditions is unknown. To overcome this limitation, we develop the Fluorescein Arsenical Hairpin Binder- (FlAsH-) based FRET in vivo approach to study DVL conformation in living cells. Using this single-cell FRET approach, we demonstrate that (i) Wnt ligands induce open DVL conformation, (ii) DVL variants that are predominantly open, show more even subcellular localization and more efficient membrane recruitment by Frizzled (FZD) and (iii) Casein kinase 1 ɛ (CK1ɛ) has a key regulatory function in DVL conformational dynamics. In silico modelling and in vitro biophysical methods explain how CK1ɛ-specific phosphorylation events control DVL conformations via modulation of the PDZ domain and its interaction with DVL C-terminus. In summary, our study describes an experimental tool for DVL conformational sampling in living cells and elucidates the essential regulatory role of CK1ɛ in DVL conformational dynamics.
Harnoš, J., Cañizal, M.C.A., Jurásek, M., Kumar, J., Holler, C., Schambony, A., Hanáková, K., Bernatík, O., Zdráhal, Z. Gömöryová, K.,Gybel’,T., Radaszkiewicz, T.W., Kravec, M., Trantírek, L., Ryneš, J., Dave, Z., Fernández-Llamazares, A.I., Vácha, R., Tripsianes, K., Hoffmann, C., and Bryja, V.: Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1, Nat. Commun. (2019) 10, 1804, 1-18. doi.org/10.1038/s41467-019-09651-7
NAT. COMMUN. 2019
Scheme of enterovirus genome release. Binding to receptors or exposure to acidic pH in endosomes induces conformational transition of virions to activated particles. The structural changes within the capsid and virus RNA enable the expulsion of pentamers from the capsid, resulting in the formation of open particles. The RNA genomes are released from the open particles. After the genome release, the pentamers may re-associate with the open capsids. Scale bar represents 10 nm
Viruses from the genus Enterovirusare important human pathogens. Receptor binding or exposure to acidic pH in endosomes converts enterovirus particles to an activated state that is required for genome release. However, the mechanism of enterovirus uncoating is not well understood. Here, we use cryo-electron microscopy to visualize virions of human echovirus 18 in the process of genome release. We discover that the exit of the RNA from the particle of echovirus 18 results in a loss of one, two, or three adjacent capsid-protein pentamers. The opening in the capsid, which is more than 120 Å in diameter, enables the release of the genome without the need to unwind its putative double-stranded RNA segments. We also detect capsids lacking pentamers during genome release from echovirus 30. Thus, our findings uncover a mechanism of enterovirus genome release that could become target for antiviral drugs
Buchta, D., Füzik, T., Hrebík, D., Levdansky, Y., Sukeník, L., Mukhamedova, L., Moravcová, J., Vácha, R., and Plevka, P: Enterovirus particles expel capsid pentamers to enable genome release, Nat. Commun. (2019)10, 1138, 1-9 doi.org/10.1038/s41467-019-09132-x