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.
Czech national centre of European Research Infrastructure Consortium INSTRUCT ERIC.
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.
Postdoc in Protein Research
A postdoc position is available in the Core Facility Biomolecular Interaction and Crystalization.
Titan Krios transmission electron microscope at CEITEC equipped with phase plate and last generation direct electron detectors
Phase plate significantly increases contrast in cryo-electron microscopy data.
CIISB Core Facilities Assist a Top-Class Research
Wednesday – Thursday
18 Apr – 19 Apr
1st annual CEITEC symposium on Recent Advances in Cryo-Electron Microscopy will gather the researchers to discuss the latest advances in cryo-electron microscopy with several world leading experts in the field.
Thursday – Saturday
22 Mar – 24 Mar
XV. Discussions in Structural Molecular Biology and the 2nd User Meeting of the Czech Infrastructure for Integrative Structural Biology
The details will be published in late October 2017 when also the registration web site will open.
Thursday – Friday
5 Apr – 6 Apr
Fragment-screening (FS) is a popular approach to identify the binding of small organic molecules (fragments) to protein targets.
Nat. Commun. 2018
Nat. Commun. 2018
Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, Pavel Plevka and his coworkers present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.
Fuzik, T. et al. Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody. Nature Communications 9, 11, doi:10.1038/s41467-018-02882-0 (2018). doi:10.1038/s41467-018-02882-0
The automation of NMR structure determination remains a significant bottleneck towards increasing the throughput and accessibility of NMR as a structural biology tool to study proteins. The chief barrier currently is that obtaining NMR assignments at sufficient levels of completeness to accurately define the structures by conventional methods requires a significant amount of spectrometer time (several weeks), and effort by a trained expert (up to several months). Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the NMR structures of proteins can be determined accurately and in an unsupervised manner in a matter of days.
4D-CHAINS software is free for non-commercial usage and can be downloaded from https://github.com/tevang/4D-CHAINS
Evangelidis, T. et al. Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra. Nature Communications 9, 13, doi:10.1038/s41467-017-02592-z (2018).