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 characterization of protein 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. Besides, the platform also offers: Identification and quantification of proteins, Precise determination of protein molecular mass, Characterization of various posttranslational modifications.
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 (or higher) deg Celsius. Dedicated rooms with stereomicroscopes for crystal manipulation are available at 20, 10 and 25 (or higher) deg Celsius. 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 provided for the analysis of kinetic and thermodynamic parameters of biomolecular interaction and for the biophysical characterisation of the structure, function and stability of biological biological macromolecules like proteins, nucleic acids, lipids and their complexes (Microscale Thermophoresis, Surface Plasmon Resonance, Isothermal titration Calorimetry, Differential Scanning Fluorescence, Differential Scanning Calorimetry, Circular Dichroism, Dynamic Light Scattering, UV/Vis Spectrometry).
D8 Venture diffractometer (Bruker) with a MetalJet D2 high-flux liquid Gallium X-ray source, Photon II detector and Kappa goniometer. This diffractometer is used for X-ray diffraction studies of biomolecular crystals (macromolecular crystallography). The device is also equipped with an ISX motorised stage for in-situ X-ray diffraction experiments, enabling screening of diffraction properties in crystallisation plates (plus limited diffraction data collection). The beam size of 70 microns (FWHM) and its high brilliance enable very effective screening, automated in-plate screening and fast data collection. Typical exposure time per degree for protein crystals: 30-90 seconds.
Versatile instrument to perform SAXS or WAXS experiments on liquid samples, in the temperature range -10° C to 120° C. SAXSpoint 2.0 (Anton Paar) is equipped with the latest high brilliance source MetalJet C2+ having a liquid gallium alloy anode, and a Dectris EIGER 1M detector. Samples can be loaded using the automated high precision sampler or manually in capillaries, including a high S/N silicon nitride measurement cell. The state of the sample can be monitored online using UV-Vis spectroscopy to identify radiation damage, measure precise sample concentration and aggregation state.