Czech Infrastructure for Integrative Structural Biology
CIISB - Czech Infrastructure for Integrative Structural Biology is formed by two Centers of Excellence for Structural Biology constructed within two projects: CEITEC – Central European Institute of Technology, Brno and BIOCEV - Biotechnology and Biomedicine Centre, Vestec, Prague-West. CEITEC and BIOCEV have been financed by the EU Structural Funds through the Operational Program Research and Development for Innovation, priority axis 1 – European Centers of Excellence, which is managed by the Ministry of Education, Youth and Sports of the Czech Republic. The Czech structural biology community is represented by the Czech Society for Structural Biology (CSSB), which is forming a national link to INSTRUCT. CIISB affiliation with INSTRUCT contributes to the development of human resources in research, attracts qualified national and international researchers, and enables efficient dissemination of knowledge and expertise within INSTRUCT, as well as the efficient use of the infrastructure.
The core facilities for structural biology in BIOCEV are organized under the Centre of molecular structure, run by the Institute of Biotechnology, Czech Academy of Sciences.
The Centre of Molecular Structure (CMS) encompasses several laboratories providing a complex approach to studies of three-dimensional structure, function and biophysical properties of biological molecules.
The BIOCEV building is located just outside of Prague. It can be easily reached by car or public transport. You will find detailed information on how to get to BIOCEV here.
Structural mass spectrometry (MS3D) offers various methodologies for characterisation of protein structure. The Institute of Biotechnology/Centre of Molecular Structure (IBT/CMS) at BIOCEV offers different labelling approaches including hydrogen/deuterium exchange, covalent labelling, chemical cross-linking and limited proteolysis. The facility is equipped with cutting-edge technologies including high-resolution mass spectrometer, HPLC system, H/D system and in-house software for data processing. The service provided includes data processing and reporting ready for publication. The platform also offers: identification and quantification of proteins, precise determination of protein molecular mass, and characterisation of various post translational modifications.
Separation of protein mixtures
Intact protein analysis
Native mass spectrometry
Characterization of protein modifications
Protein surface covalent labelling
Hydrogen/deuterium exchange (HDX)
Data processing and interpretation of mass spectrometric data
Crystallization of Proteins and Nucleic Acids core facility provides services focused on obtaining crystals of biomacromolecules and their complexes. We support both manual and robotic crystallization drops setting under various conditions. Remote control of crystal growth in the crystallization hotel is provided using the web interface over Internet.
The macromolecular crystallisation platform enables in-drop dynamic light scattering measurement to check the quality of the protein sample, robotic setup of 96-well crystallisation plates, incubation at selected temperature from a wide range, and automated monitoring of the crystallisation experiments. Experiments can be stored at 4-30°C (or higher). Dedicated rooms with stereomicroscopes for crystal manipulation are available at 20°C, 10°C and 25°C (or higher). Inert atmosphere crystallisation is available. Equipment: Formulatrix NT8 Dropsetter, Art Robbins Gryphon Dropsetter, DLS Spectrolight 600, Glovebox PETG10R320T3, Formulatrix RI 1000 Crystallisation Hotel, stereomicroscopes with imaging, cooled centrifuges, nanodrop spectrophotometer.
Techniques are available for the analysis of kinetic and thermodynamic parameters of biomolecular interactions and for the biophysical characterisation of the structure, function and stability of biological biological macromolecules like proteins, nucleic acids, lipids and their complexes.
Characterization of intermolecular interactions by MST, iTC and SPR and evaluation of conformation of DNA, secondary structure of proteins, thermodynamic parameters of temperature transition, stability of biomolecules by CD and UV/Vis spectrometry, spectrofluorimetry, FTIR, DSC, DLS, MALDS and DSF.
Diffraction techniques core facility provides services for characterization of protein structure using single crystal X-ray diffraction and small-angle X ray scattering for analysis of liquid samples. The quality of high-intense X-ray beams is enabled by using of MetalJet sources (Excillum). The service provided includes data processing and reporting ready for publication.
Screening for X-ray diffraction of macromolecules
In-house data collection and processing
In-situ evaluation of sensitive crystallization targets, experimental phasing experiments – evaluation for MIR, SAD and MAD approaches
SAXS data measurement and evaluation
Synchrotron-based data collection and processing, structure solution