|
Preparing for the Evaluation of Large Research Infrastructures
As spring awakens the world around us with fresh energy, we too are entering an important phase in the life of our infrastructure—one filled with opportunity, planning, and preparation for the future.
We eagerly await the official guidelines from the Ministry of Education, Youth, and Sports (MEYS) for this year’s evaluation of large research infrastructures. This critical assessment will inform updates to the national Roadmap and guide government decisions regarding budget allocations for the 2027–2034 period. Securing this funding is essential for the long-term sustainability of CIISB, and we are fully committed to excelling in the evaluation process.
|
|
|
|
The CIISB Executive Committee convened during the XXI Discussions in Structural Molecular Biology and the 8th CIISB User Meeting, held in Nové Hrady from March 20–22, 2025. These meetings provided a valuable forum to review investment plans and operational budgets for the coming years, and to reflect on the future direction of our infrastructure based on insightful input from the Scientific Advisory Board (SAB).
Thanks to ongoing support from the Ministry of Education, Youth and Sports (MEYS)—specifically through Project LM2023042 and the European Regional Development Fund initiative Innovation of Czech Infrastructure for Integrative Structural Biology (No. CZ.02.01.01/00/23_015/0008175)—our facilities continue to expand their capabilities by introducing new services and cutting-edge equipment.
Key recent upgrades include the installation of a new mass spectrophotometer at the Biomolecular Interactions Core Facility, a cryo-FIB/SEM microscope for cryo-volume EM at the Cryo-Electron Microscopy Facility, and a single-cell mass spectrometry system at the Proteomics Facility. In addition, the Protein Production Facility has expanded its services to include protein production in HEK293 and Sf9 cells.
|
|
|
|
|
Applications 2024
- 151 internal applications
- 117 external applications (Czech)
- 57 applications from foreign users
You can find more information here.
|
|
|
| |
2021 |
2022 |
2023 |
2024 |
| Internal users |
166 |
129 |
135 |
151 |
| External users |
69 |
79 |
88 |
117 |
| Foreign users |
16 |
27 |
40 |
57 |
| Total |
251 |
235 |
263 |
237 |
|
|
|
|
|
|
We're excited to invite you to join us at the CTLS 2025 Congress happening in the beautiful city of Brno from 10-12 June 2025! This gathering is going to be an excellent opportunity, bringing together core facility administrators, managers, researchers, and professionals to talk, collaborate, and dive into why core facilities are key to shaping the scientific world. Don't miss out and check the congress website, where all the information are being published!
|
|
|
CIISB meeting of managerial bodies 14. 11. 2024
|
|
|
On November 14, 2024, all CIISB management bodies met to listen to the current status of the research infrastructure and its core facilities at CEITEC - Central European Institute of Technology and Institute of Biotechnology.
The meeting was held in hybrid mode as most of our SAB members are foreign renowned researchers. Altogether, SAB members, Executive Committee members, Supervisory Board members, and CF Heads were informed about the latest achievements (user publications, open access applications, educational activities, etc.), upcoming evaluations from MEYS and Instruct-ERIC, and current financing by national and Horizon projects. All 10 CF Heads presented their services portfolio, future plans in equipment upgrade and method development, and significant user cases.
Memorial Conference of Prof. Vladi Sklenář, CIISB father-founder followed this meeting.
|
|
|
Vladimír Sklenář Scholarship
|
|
|
To honor the memory of Prof. Vladimír Sklenář, an internationally renowned scientist and an important organizer of scientific activities in the Czech Republic, CEITEC Masaryk University is introducing the Vladimír Sklenář Scholarship. The scholarship is intended for students of doctoral studies at universities in the Czech and Slovak Republics working in the field of NMR spectroscopy, and can be used to cover the costs related to their studies. The intention is to strengthen and improve the quality of studies, as well as personal and career development.
The scholarship in the amount of CZK 100,000, which may be taxable according to the practice of the institution and/or the tax regulations of the beneficiary's country, is sponsored by Měřící technika Morava. The scholarship will be awarded to one person per year.
|
|
|
The memory of Josef Dadok lives on at CEITEC through cutting-edge research in spectroscopy
|
|
|
On October 4, 2024, Professor Josef Dadok, the founder of nuclear magnetic resonance (NMR) in Czechoslovakia and a prominent figure in the field internationally, died in the United States at the age of 98. Professor Dadok worked in Brno in the 1950s and 1960s, where he led the development of the first NMR spectrometers at the Institute of Instrumentation of the Czechoslovak Academy of Sciences, later mass-produced by the national company Tesla Brno, making Czechoslovakia one of the world leaders in this field.
|
|
|
Meet Petr Pompach, Head of CF Structural Mass Spectrometry at BTÚ
|
|
|
|
My path to leading the Structural Mass Spectrometry Core Facility at Biocev was driven by a passion for both technology and discovery. Mass spectrometry is a unique field where analytical precision meets biological complexity, allowing us to uncover molecular structures and interactions. I was drawn to this role because it offers the opportunity to push scientific boundaries, support innovative research, and collaborate with experts across disciplines—all while ensuring that our facility remains at the forefront of mass spectrometry advancements.
Of course, leading a core facility comes with challenges. The rapidly evolving nature of mass spectrometry requires constant adaptation—staying ahead of new methodologies, optimizing workflows, and ensuring the highest quality of data for researchers. Balancing administrative responsibilities with scientific innovation is another hurdle, but one that keeps the role dynamic and engaging.
To clear my mind, I turn to nature and endurance sports. Orienteering and cross-country running offer a perfect escape—demanding both physical endurance and strategic thinking, much like my work in the lab. These activities help me reset, offering clarity and fresh perspectives that I bring back to my research.
For me, leading this core facility is about more than managing instruments and data—it's about fostering collaboration, advancing science, and uncovering the molecular secrets.
|
|
|
New services in Protein production core facility
|
|
|
|
We are pleased to announce the expansion of our Protein Production Core Facility with the introduction of eukaryotic protein production. In addition to prokaryotic expression in E. coli, we now offer protein production in human embryonic kidney cells (HEK) and Sf9 insect cells.
|
|
|
New instrumentation in Proteomics core facility
|
|
|
|
In March, two new high resolution mass spectrometers were installed in our core facility thanks to CIISB project (CZ.02.01.01/00/23_015/0008175). First we upgraded our timsTOF Pro 2 instrument to timsTOF HT improving our performance in whole proteome analyses with faster scanning speed and a wider dynamic range. In second, Ultra 2 mass spectrometer was installed. This timsTOF instrument opens doors to deeper analysis of samples with limited amount of input material due to its ultimate sensitivity.
|
|
|
Availability of cryo-volume imaging services facilitated through installation of high-resolution cryo-pFIB/SEM microscope at CEITEC Masaryk University
|
|
Cryo-electron microscopy core facility at CEITEC MUNI has finished installation of a new focused ion beam scanning electron microscope (FIB/SEM). BioHydra (ThermoScientific, Helios Hydra V) is equipped with an immersion SEM optics for high-resolution SEM imaging under room-temperature and cryogenic conditions and FIB working on the principle of inductively-couple plasma with a four gas (Xe,Ar,O,N) source for efficient material ablation. The instrument was proven to deliver 3D reconstruction of whole eukaryotic cells or parts of a tissue preserved at near-native state at resolution better than 30nm. Thus, BioHydra will provide the CIISB user community access to the cryo-volume imaging technology which is rapidly developing over the last few years and extend the capacity of cellular lamellae preparation for in situ structural biology studies by cryo-electron tomography. The installation of BioHydra microscope was made possible through the "Innovation of Czech Infrastructure for Integrative Structural Biology" grant, funded by the OP JAK for Research Infrastructures I.
|
|
|
|
Two cutting-edge instruments in CF BIC
|
|
|
The Biomolecular Interactions and Crystallography Core Facility of CEITEC MU is very happy to announce the installation of two cutting-edge instruments that will significantly boost our research capabilities to explore molecular properties with greater precision and depth.
|
|
|
Analysis of micro and nanoplastic particles in Nanobio Core Facility
|
|
CF Nanobio offers the analysis of micro and nano plastic particles that pose risks to ecosystems and human health. Raman microscopy enables detailed chemical analysis of these particles in water, milk, blood, tissues, soil, and food. Semi-automated analysis using Particle Analysis software and an extensive polymer library ensures precise identification and quantification. The Renishaw InVia Raman microscope, with upgraded lasers and polarization capabilities, supports diverse applications.
|
|
|
Enhanced SAXS Instrumentation: MetalJet D2+ Upgrade Boosts Performance and Beam Intensity
|
|
|
In CF Diffraction Techniques, we have successfully upgraded the X-ray source of the SAXS instrument. The upgrade of MetalJet C2 to D2+ brought more than double intensity of the primary beam. The instrument enables rapid standard SAXS measurements with a low volume autosampler, SEC-SAXS experiments or special applications, now with substantially improved signal to noise ratio.
|
|
|
New mass photometer in CF BIC
|
|
|
The Biomolecular Interactions and Crystallography Core Facility of CEITEC MU is very happy to announce the installation of a new cutting-edge instrument that will assist in the characterization of macromolecular complexes. Mass photometer TwoMP (Refeyn) is designed to precisely determine the molecular mass of proteins, nucleic acids, and other macromolecules in a broad range of sizes. The machine is equipped with a recently developed fluidics system, allowing to analyze both high- and low-stability complexes across various concentrations. The instrument will be operated in user mode and shall be available by the end of the year.
|
|
|
CIISB Research Highlights
|
|
Nucleic Acid Research 2025
|
|
|
Cryo-EM structure of 30S–30S dimer formed by aRDF protein.
Gabriel Demo Research Group
Significance
Protein synthesis (translation) consumes a substantial proportion of cellular resources, prompting specialized mechanisms to reduce translation under adverse conditions. Ribosome inactivation often involves ribosome-interacting proteins. In both bacteria and eukaryotes, various ribosome-interacting proteins facilitate ribosome dimerization or hibernation, and/or prevent ribosomal subunits from associating, enabling the organisms to adapt to stress. Despite extensive studies on bacteria and eukaryotes, understanding factor-mediated ribosome dimerization or anti-association in archaea remains elusive. Here, we present cryo-electron microscopy structures of an archaeal 30S dimer complexed with an archaeal ribosome dimerization factor (designated aRDF), from Pyrococcus furiosus, resolved at a resolution of 3.2 Å. The complex features two 30S subunits stabilized by aRDF homodimers in a unique head-to-body architecture, which differs from the disome architecture observed during hibernation in bacteria and eukaryotes. aRDF interacts directly with eS32 ribosomal protein, which is essential for subunit association. The binding mode of aRDF elucidates its anti-association properties, which prevent the assembly of archaeal 70S ribosomes.
Hassan, et al.: Novel archaeal ribosome dimerization factor facilitating unique 30S–30S dimerization
Nucleic Acids Research 2025, 53(2), DOI: 10.1093/nar/gkae1324
|
|
|
|
|
|
Electrostatic potential of unphosphorylated and phosphorylated MAP2c.
Lukáš Žídek Research Group
Significance
Microtubule associated protein 2 (MAP2) interacts with the regulatory protein 14-3-3ζ in a cAMP-dependent protein kinase (PKA) phosphorylation dependent manner. Using selective phosphorylation, calorimetry, nuclear magnetic resonance, chemical crosslinking, and X-ray crystallography, we characterized interactions of 14-3-3ζ with various binding regions of MAP2c. Although PKA phosphorylation increases the affinity of MAP2c for 14-3-3ζ in the proline rich region and C-terminal domain, unphosphorylated MAP2c also binds the dimeric 14-3-3ζ via its microtubule binding domain and variable central domain. Monomerization of 14-3-3ζ leads to the loss of affinity for the unphosphorylated residues. In neuroblastoma cell extract, MAP2c is heavily phosphorylated by PKA and the proline kinase ERK2. Although 14-3-3ζ dimer or monomer do not interact with the residues phosphorylated by ERK2, ERK2 phosphorylation of MAP2c in the C-terminal domain reduces the binding of MAP2c to both oligomeric variants of 14-3-3ζ.
Jansen, et al.: Characterization of multiple binding sites on microtubule associated protein 2c recognized by dimeric and monomeric 14‐3‐3ζ
The FEBS Journal, DOI: 10.1111/febs.17405
|
|
|
|
|
|
|
The scheme of the variational autoencoder-based pipeline for the design of novel sequences.
Loschmidt Laboratories
Significance
Enzymes play a crucial role in sustainable industrial applications, with their optimization posing a formidable challenge due to the intricate interplay among residues. Computational methodologies predominantly rely on evolutionary insights of homologous sequences. However, deciphering the evolutionary variability and complex dependencies among residues presents substantial hurdles. Here, we present a new machine-learning method based on variational autoencoders and evolutionary sampling strategy to address those limitations. We customized our method to generate novel sequences of model enzymes, haloalkane dehalogenases. Three design–build–test cycles improved the solubility of variants from 11% to 75%. Thorough experimental validation including the microfluidic device MicroPEX resulted in 20 multiple-point variants. Nine of them, sharing as little as 67% sequence similarity with the template, showed a melting temperature increase of up to 9 °C and an average improvement of 3 °C. The most stable variant demonstrated a 3.5-fold increase in activity compared to the template. High-quality experimental data collected with 20 variants represent a valuable data set for the critical validation of novel protein design approaches. Python scripts, jupyter notebooks, and data sets are available on GitHub (https://github.com/loschmidt/vae-dehalogenases), and interactive calculations will be possible via https://loschmidt.chemi.muni.cz/fireprotasr/.
Kohout, et al.: Engineering Dehalogenase Enzymes Using Variational Autoencoder-Generated Latent Spaces and Microfluidics
JACS Au 5 2025, 5(2), DOI: 10.1021/jacsau.4c01101
|
|
|
Nature Communications 2025
|
|
|
|
RECQ4 cooperates with MUS81 to prevent ultrafine bridges formation.
Lumír Krejčí Research Group
Significance
Replication stress, particularly in hard-to-replicate regions such as telomeres and centromeres, leads to the accumulation of replication intermediates that must be processed to ensure proper chromosome segregation. In this study, we identify a critical role for the interaction between RECQ4 and MUS81 in managing such stress. We show that RECQ4 physically interacts with MUS81, targeting it to specific DNA substrates and enhancing its endonuclease activity. Loss of this interaction, results in significant chromosomal segregation defects, including the accumulation of micronuclei, anaphase bridges, and ultrafine bridges (UFBs). Our data further demonstrate that the RECQ4-MUS81 interaction plays an important role in ALT-positive cells, where MUS81 foci primarily colocalise with telomeres, highlighting its role in telomere maintenance. We also observe that a mutation associated with Rothmund-Thomson syndrome, which produces a truncated RECQ4 unable to interact with MUS81, recapitulates these chromosome instability phenotypes. This underscores the importance of RECQ4-MUS81 in safeguarding genome integrity and suggests potential implications for human disease. Our findings demonstrate the RECQ4-MUS81 interaction as a key mechanism in alleviating replication stress at hard-to-replicate regions and highlight its relevance in pathological conditions such as RTS.
Ashraf, et al.: RECQ4-MUS81 interaction contributes to telomere maintenance with implications to Rothmund-Thomson syndrome
Nature Communications 2025, 16, DOI: 10.1038/s41467-025-56518-1
|
|
|
|
|
|
|
|
R. Obořilová, et al.: Piezoelectric biosensor with dissipation monitoring enables the analysis of bacterial lytic agent activity, Scientific Reports, 15 (2025) 1, 10.1038/s41598-024-85064-x
D. Radhakrishnan, et al.: Deubiquitinase BAP1 is crucial for surface expression of T cell receptor (TCR) complex, T cell-B cell conjugate formation, and T cell activation, J. Leukoc. Biol., (2025) 12, 10.1093/jleuko/qiae184
A. Dikunova, et al.: Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms, Structure, 33 (2025) 2, 10.1016/j.str.2024.11.010
E. Slivenecka, et al.: The Actinobacillus pleuropneumoniae apxIV operon encodes an antibacterial toxin-immunity pair, Microbiological Research, 292 (2025), 10.1016/j.micres.2024.128043
E. Birgusova, et al.: TP53 detection based on electrochemical genosensors with different types of gold nanoparticles, Microchemical Journal, 209 (2025), 10.1016/j.microc.2025.112856
R. Ashraf, et al.: RECQ4-MUS81 interaction contributes to telomere maintenance with implications to Rothmund-Thomson syndrome, Nature Communications, 16 (2025), 10.1038/s41467-025-56518-1
J. Rynes, et al.: Protein structure and interactions elucidated with in-cell NMR for different cell cycle phases and in 3D human tissue models, Communications Biology, 8 (2025) 1, 10.1038/s42003-025-07607-w
J. Planas-Iglesias, et al.: Automated Engineering Protein Dynamics via Loop Grafting Renilla Luciferase Catalysis: Improving Renilla Luciferase Catalysis, ACS Catalysis, 15 (2025) 4, 10.1021/acscatal.4c06207
K. Snopková, et al.: Pseudomonas rossensis sp. nov., a novel psychrotolerant species produces antimicrobial agents targeting resistant clinical isolates of Pseudomonas aeruginosa, Current Research in Microbial Sciences, 8 (2025), 10.1016/j.crmicr.2025.100353
M. Schäfer, et al.: Structure–Activity Relationships and Biological Insights into PSMA-617 and Its Derivatives with Modified Lipophilic Linker Regions, ACS Omega, 10 (2025) 7, 10.1021/acsomega.4c10142
D. Brandis, et al.: The Internal Structural Dynamics of Elastin-Like Polypeptide Assemblies by 13 C-Direct Detected NMR Spectroscopy, Analytical Chemistry, 97 (2025) 7, 10.1021/acs.analchem.4c05163
S. Šreibr, et al.: Characterization of Heterorhabditis bacteriophora response to insect-derived and non-biological stimuli: Insights into nematode recovery and released proteins, Pesticide Biochemistry and Physiology, 208 (2025), 10.1016/j.pestbp.2025.106318
A. Náplavová, et al.: Harnessing the power of 19F NMR for characterizing dimerization and ligand binding of 14-3-3 proteins, International Journal of Biological Macromolecules, 305 (2025), 10.1016/j.ijbiomac.2025.141253
J. Torrisi, et al.: Anion Transport by Bambusuril‐Bile Acid Conjugates: Drastic Effect of the Cholesterol Content, Angewandte Chemie International Edition, 64 (2025) 9, 10.1002/anie.202424754
J. Blazickova, et al.: Overlapping and separable activities of BRA-2 and HIM-17 promote occurrence and regulation of pairing and synapsis during Caenorhabditis elegans meiosis, Nature Communications, 16 (2025) 1, 10.1038/s41467-025-57862-y
|
|
|
|
|
