Změnit instituci

Centrální laboratoř Interakce a krystalizace biomolekul

PŘÍSTUP DO REZERVAČNÍHO SYSTÉMU pro registrované uživatele (pro REGISTRACI klikněte ZDE)

Head of Core Facility
Researcher ID
Telefon: +420 54949 3805, +420 54949 8166
E-mail:
Kancelář:

Oficiální Email: bic@ceitec.muni.cz


Hlavní činnost 

Sdílená laboratoř poskytuje služby umožňující strukturní charakterizaci biomolekul a studium (bio)molekulárních interakcí v reálném čase především pomocí metod založených na biosenzorech a kalorimetrii. Přístrojové vybavení laboratoře umožňuje studium podmínek pro krystalizaci biomolekul a jejich komplexů, základní charakterizaci biofyzikálních vlastností molekul (analytická ultracentrifugace, dynamický rozptyl světla, CD spektroskopie, diferenciální skenovací kalorimetrie) a studium termodynamiky a/nebo kinetiky vzájemných interakcí (isotermická titrační kalorimetrie, resonance povrchového plasmonu, CD spektroskopie, analytická ultracentrifugace).

Unikátní možnosti 

  • Nasazení screeningových krystalizačních misek (96-ti jamkové UVP misky se třemi pozicemi sedící kapky pro jednu podmínku) pomocí komerčně dostupných kitů (až 13 tisíc podmínek)
  • Automatická kontrola všech krystalizačních kapek vzdálený přístup k výsledkům pro uživatele
  • UV zobrazování pro odlišení proteinů od solí
  • Nasazení optimalizačních krystalizačních misek (24  jamkové, 96-ti jamkové) příprava vícerozměrných gradientů z až 5-ti různých roztoků)
  • Stanovení fázového diagramu precipitace proteinů
  • Příprava krystalů pro určení struktury pomocí rentgenové difrakce
  • Zlepšování kvality krystalů pro strukturní studie
  • Isotermická titrační mikrokalorimetrie
  • Diferenciální skenovací kalorimetrie
  • Resonance povrchového plasmonu
  • Analýza velikosti částic
  • Analytická ultracentrifugace
  • Cirkulární dichroismus, měření fluorescence

Základní přístrojové vybavení

cf interakce banner cz small

Sdílená laboratoř je součástí českého národního přidruženého centra INSTRUCT a členem celoevropského sdružení ARBRE (Association of Resources for Biophysical Research in Europe)

Všechny sdílené laboratoře CEITEC jsou k dispozici externím uživatelům (z akademického prostředí i z firem). Čeští i zahraniční výzkumníci z univerzit a výzkumných institucí, kteří mají zájem o získání přístupu do sdílených laboratoří, mohou využít podpory z  výzkumné infrastruktury CIISB, financované Ministerstvem školství, mládeže a tělovýchovy ČR.

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seznam / vizitky

Jméno a pozice

E-mail

Telefon

prof. RNDr. Michaela Wimmerová, Ph.D.
docentka, manažerka pro koordinaci a správu projektů, vedoucí pracoviště
+420 54949 3805, +420 54949 8166
Mgr. Eva Dubská
odborná pracovnice
+420 54949 2527
Mgr. Josef Houser, Ph.D.
odborný pracovník ve výzkumu
+420 54949 2527
Mgr. Jan Komárek
odborný pracovník - PhD student
+420 54949 6011
Mgr. Jana Kosourová
odborná pracovnice
+420 54949 8201, +420 54949 8314
Mgr. Lenka Malinovská, Ph.D.
odborná pracovnice ve výzkumu
+420 54949 7646, +420 54949 2527
Mgr. Marie Pokorná
odborná pracovnice
+420 54949 5901
Mgr. Jitka Ždánská
odborná pracovnice
+420 54949 2527

VYBRANÉ PUBLIKACE

2017

  • HOUSER, J; KOZMON, S; MISHRA, D; MISHRA, SK; ROMANO, PR; WIMMEROVA, M; KOCA, J, 2017:Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL. PLOS ONE 12 (12)
  • JANCARIKOVA, G; HOUSER, J; DOBES, P; DEMO, G; HYRSL, P; WIMMEROVA, M, 2017:Characterization of novel bangle lectin from Photorhabdus asymbiotica with dual sugar-binding specificity and its effect on host immunity. PLOS PATHOGENS 13 (8)

2016

  • FUJDIAROVA, E; GAJDOS, L; WIMMEROVA, M, 2016:Study of lectins from Photorhabdus luminescens to reveal their function in P. luminescens life cycle. FEBS JOURNAL 283 , p. 152 - 152.
  • KERR, SC; FISCHER, GJ; SINHA, M; MCCABE, O; PALMER, JM; CHOERA, T; LIM, FY; WIMMEROVA, M; CARRINGTON, SD; YUAN, SP; LOWELL, CA; OSCARSON, S; KELLER, NP; FAHY, JV, 2016:FleA Expression in Aspergillus fumigatus Is Recognized by Fucosylated Structures on Mucins and Macrophages to Prevent Lung Infection. PLOS PATHOGENS 12 (4)
  • KUMAR, A; SYKOROVA, P; DEMO, G; DOBES, P; HYRSL, P; WIMMEROVA, M, 2016:A Novel Fucose-binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure. JOURNAL OF BIOLOGICAL CHEMISTRY 291 (48), p. 25032 - 25049.
  • NORTON, P; COMUNALE, MA; HERRERA, H; WANG, MJ; HOUSER, J; WIMMEROVA, M; ROMANO, PR; MEHTA, A, 2016:Development and application of a novel recombinant Aleuria aurantia lectin with enhanced core fucose binding for identification of glycoprotein biomarkers of hepatocellular carcinoma. PROTEOMICS 16 (24), p. 3126 - 3136.

2015

  • HOUSER, J; KOMAREK, J; CIOCI, G; VARROT, A; IMBERTY, A; WIMMEROVA, M, 2015:Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 71 , p. 442 - 453.
  • SEHNAL, D; VAREKOVA, RS; PRAVDA, L; IONESCU, CM; GEIDL, S; HORSKY, V; JAISWAL, D; WIMMEROVA, M; KOCA, J, 2015:ValidatorDB: database of up-to-date validation results for ligands and non-standard residues from the Protein Data Bank. NUCLEIC ACIDS RESEARCH 43 (D1), p. D369 - D375.

2014

  • ADAMOVA, L; MALINOVSKA, L; WIMMEROVA, M, 2014:New Sensitive Detection Method for Lectin Hemagglutination using Microscopy. MICROSCOPY RESEARCH AND TECHNIQUE 77 (10), p. 841 - 849.
  • DEMO, G; PAPOUSKOVA, V; KOMAREK, J; KADERAVEK, P; OTRUSINOVA, O; SRB, P; RABATINOVA, A; KRASNY, L; ZIDEK, L; SKLENAR, V; WIMMEROVA, M, 2014:X-ray vs. NMR structure of N-terminal domain of delta-subunit of RNA polymerase. JOURNAL OF STRUCTURAL BIOLOGY 187 (2), p. 174 - 186.
  • KRIZ, Z; ADAM, J; MRAZKOVA, J; ZOTOS, P; CHATZIPAVLOU, T; WIMMEROVA, M; KOCA, J, 2014:Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity. JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN 28 (9), p. 951 - 960.
  • VAREKOVA, RS; JAISWAL, D; SEHNAL, D; IONESCU, CM; GEIDL, S; PRAVDA, L; HORSKY, V; WIMMEROVA, M; KOCA, J, 2014:MotiveValidator: interactive web-based validation of ligand and residue structure in biomolecular complexes. NUCLEIC ACIDS RESEARCH 42 (W1), p. W227 - W233.

2013

  • DEMO, G; FLIEDROVA, B; WEIGNEROVA, L; WIMMEROVA, M, 2013:Crystallization and preliminary X-ray crystallographic analysis of recombinant -mannosidase from Aspergillus niger. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 69 , p. 288 - 291.
  • HOUSER, J; KOMAREK, J; KOSTLANOVA, N; CIOCI, G; VARROT, A; KERR, SC; LAHMANN, M; BALLOY, V; FAHY, JV; CHIGNARD, M; IMBERTY, A; WIMMEROVA, M, 2013:A Soluble Fucose-Specific Lectin from Aspergillus fumigatus Conidia - Structure, Specificity and Possible Role in Fungal Pathogenicity. PLOS ONE 8 (12)
  • TVAROSKA, I; KOZMON, S; WIMMEROVA, M; KOCA, J, 2013:A QM/MM Investigation of the Catalytic Mechanism of Metal-Ion-Independent Core 2 beta 1,6-N-Acetylglucosaminyltransferase. CHEMISTRY-A EUROPEAN JOURNAL 19 (25), p. 8153 - 8162.

2012

  • AUDFRAY, A; CLAUDINON, J; ABOUNIT, S; RUVOEN-CLOUET, N; LARSON, G; SMITH, DF; WIMMEROVA, M; LE PENDU, J; ROMER, W; VARROT, A; IMBERTY, A, 2012:Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes. JOURNAL OF BIOLOGICAL CHEMISTRY 287 (6), p. 4335 - 4347.
  • CECIONI, S; PRALY, JP; MATTHEWS, SE; WIMMEROVA, M; IMBERTY, A; VIDAL, S, 2012:Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm. CHEMISTRY-A EUROPEAN JOURNAL 18 (20), p. 6250 - 6263.
  • FROMMEL, J; SOURAL, M; TYLICHOVA, M; KOPECNY, D; DEMO, G; WIMMEROVA, M; SEBELA, M, 2012:Plant aminoaldehyde dehydrogenases oxidize a wide range of nitrogenous heterocyclic aldehydes. AMINO ACIDS 43 (3), p. 1189 - 1202.
  • HOUSER, J.;J. KOMAREK;N. KOSTLANOVA;G. CIOCI;A. IMBERTY;M. WIMMEROVA., 2012:Protein oligomerization in Aleuria aurantia lectin family - importance and difficulties. Materials Structure in Chemistry 19 , p. 20 - 21.
  • MARCHETTI, R; MALINOVSKA, L; LAMEIGNERE, E; ADAMOVA, L; DE CASTRO, C; CIOCI, G; STANETTY, C; KOSMA, P; MOLINARO, A; WIMMEROVA, M; IMBERTY, A; SILIPO, A, 2012:Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide. GLYCOBIOLOGY 22 (10), p. 1387 - 1398.
  • MISHRA, S; ADAMOVA, L; ADAM, J; WIMMEROVA, M; KOCA, J, 2012:Comparison of Docking Software to Predict Saccharide Binding to Proteins Combination with In silico Protein Engineering. GLYCOBIOLOGY 22 (11), p. 1648 - 1649.
  • MISHRA, SK; ADAM, J; WIMMEROVA, M; KOCA, J, 2012:In Silico Mutagenesis and Docking Study of Ralstonia solanacearum RSL Lectin: Performance of Docking Software To Predict Saccharide Binding. JOURNAL OF CHEMICAL INFORMATION AND MODELING 52 (5), p. 1250 - 1261.
  • SEHNAL, D; VAREKOVA, RS; HUBER, HJ; GEIDL, S; IONESCU, CM; WIMMEROVA, M; KOCA, J, 2012:SiteBinder: An Improved Approach for Comparing Multiple Protein Structural Motifs. JOURNAL OF CHEMICAL INFORMATION AND MODELING 52 (2), p. 343 - 359.
  • TVAROSKA, I; KOZMON, S; WIMMEROVA, M; KOCA, J, 2012:Substrate-Assisted Catalytic Mechanism of O-GIcNAc Transferase Discovered by Quantum Mechanics/Molecular Mechanics Investigation. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 134 (37), p. 15563 - 15571.
  • VISACKA, K; HOFR, C; WILLCOX, S; NECASOVA, I; PAVLOUSKOVA, J; SEPSIOVA, R; WIMMEROVA, M; SIMONICOVA, L; NOSEK, J; FAJKUS, J; GRIFFITH, JD; TOMASKA, L, 2012:Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres. JOURNAL OF BIOLOGICAL CHEMISTRY 287 (38), p. 32206 - 32215.
  • WIMMEROVA, M; KOZMON, S; NECASOVA, I; MISHRA, SK; KOMAREK, J; KOCA, J, 2012:Stacking Interactions between Carbohydrate and Protein Quantified by Combination of Theoretical and Experimental Methods. PLOS ONE 7 (10)

2011

  • CECIONI, S; FAURE, S; DARBOST, U; BONNAMOUR, I; PARROT-LOPEZ, H; ROY, O; TAILLEFUMIER, C; WIMMEROVA, M; PRALY, JP; IMBERTY, A; VIDAL, S, 2011:Selectivity among Two Lectins: Probing the Effect of Topology, Multivalency and Flexibility of "Clicked" Multivalent Glycoclusters. CHEMISTRY-A EUROPEAN JOURNAL 17 (7), p. 2146 - 2159.
  • GILBOA-GARBER, N; ZINGER-YOSOVICH, KD; SUDAKEVITZ, D; LERRER, B; IMBERTY, A; WIMMEROVA, M; WU, AM; GARBER, NC, 2011:The Five Bacterial Lectins: PA-II, PA-III, RSL, RS-III and CV-III Interactions with Diverse Animal Cells and Glycoproteins. Advances in Experimental Medicine and Biology 705 , p. 155 - 211.
  • HAVEL, V; SVEC, J; WIMMEROVA, M; DUSEK, M; POJAROVA, M; SINDELAR, V, 2011:Bambus[n]urils: a New Family of Macrocyclic Anion Receptors. ORGANIC LETTERS 13 (15), p. 4000 - 4003.
  • REVESZ, A; SCHRODER, D; SVEC, J; WIMMEROVA, M; SINDELAR, V, 2011:Anion Binding by Bambus[6]uril Probed in the Gas Phase and in Solution. JOURNAL OF PHYSICAL CHEMISTRY A 115 (41), p. 11378 - 11386.
  • SULAK, O; CIOCI, G; LAMEIGNERE, E; BALLOY, V; ROUND, A; GUTSCHE, I; MALINOVSKA, L; CHIGNARD, M; KOSMA, P; AUBERT, DF; MAROLDA, CL; VALVANO, MA; WIMMEROVA, M; IMBERTY, A, 2011:Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity. PLOS PATHOGENS 7 (9)

2010

  • KLUMPLER, T; SEDLACEK, V; MAREK, J; WIMMEROVA, M; KUCERA, I, 2010:Crystallization and initial X-ray diffraction studies of the flavoenzyme NAD(P)H:(acceptor) oxidoreductase (FerB) from the soil bacterium Paracoccus denitrificans. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 66 , p. 431 - 434.
  • LAMEIGNERE, E; SHIAO, TC; ROY, R; WIMMEROVA, M; DUBREUIL, F; VARROT, A; IMBERTY, A, 2010:Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin. GLYCOBIOLOGY 20 (1), p. 87 - 98.
  • MISHRA, NK; KRIZ, Z; WIMMEROVA, M; KOCA, J, 2010:Recognition of selected monosaccharides by Pseudomonas aeruginosa Lectin II analyzed by molecular dynamics and free energy calculations. CARBOHYDRATE RESEARCH 345 (10), p. 1432 - 1441.
  • SULAK, O; CIOCI, G; DELIA, M; LAHMANN, M; VARROT, A; IMBERTY, A; WIMMEROVA, M, 2010:A TNF-like Trimeric Lectin Domain from Burkholdeda cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens. STRUCTURE 18 (1), p. 59 - 72.

2009

  • HANSEN, SF; BETTLER, E; WIMMEROVA, M; IMBERTY, A; LEROUXEL, O; BRETON, C, 2009:Combination of Several Bioinformatics Approaches for the Identification of New Putative Glycosyltransferases in Arabidopsis. JOURNAL OF PROTEOME RESEARCH 8 (2), p. 743 - 753.
  • HOFR, C., SULTESOVA, P., ZIMMERMANN, M., MOZGOVA, I., SCHRUMPFOVA, P. P., WIMMEROVA, M., FAJKUS, J.,, 2009:Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specificity and kinetics. BIOCHEMICAL JOURNAL 419 , p. 221 - 228.
  • CHEMANI, C; IMBERTY, A; DE BENTZMANN, S; PIERRE, M; WIMMEROVA, M; GUERY, BP; FAURE, K, 2009:Role of LecA and LecB Lectins in Pseudomonas aeruginosa-Induced Lung Injury and Effect of Carbohydrate Ligands. INFECTION AND IMMUNITY 77 (5), p. 2065 - 2075.
  • MATEJKOVA, M; ZIDKOVA, J; ZIDEK, L; WIMMEROVA, M; CHMELIK, J; SKLENAR, V, 2009:Investigation of Thermal Denaturation of Barley Nonspecific Lipid Transfer Protein 1 (ns-LTP1b) by Nuclear Magnetic Resonance and Differential Scanning Calorimetry. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 57 (18), p. 8444 - 8452.
  • TESARIK, R; SEDLACEK, V; PLOCKOVA, J; WIMMEROVA, M; TURANEK, J; KUCERA, I, 2009:Heterologous expression and molecular characterization of the NAD(P)H:acceptor oxidoreductase (FerB) of Paracoccus denitrificans. PROTEIN EXPRESSION AND PURIFICATION 68 (2), p. 233 - 238.
  • WIMMEROVA, M; MISHRA, NK; POKORNA, M; KOCA, J, 2009:Importance of oligomerisation on Pseudomonas aeruginosa Lectin-II binding affinity. In silico and in vitro mutagenesis. JOURNAL OF MOLECULAR MODELING 15 (6), p. 673 - 679.

PROJEKTY

  • RIAT-CZ (ATCZ40), Interreg CZ-AT, 2016 - 2018
  • CIISB4HEALTH - Česká infrastruktura pro integrativní strukturní biologii pro lidské zdraví (CZ.02.1.01/0.0/0.0/16_013/0001776), MEYS, 2017 - 2021
  • CIISB - České centrum pro integrativní strukturní biologii (LM2015043), MEYS, 2016 - 2019
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Equipment Research group / CF Profile card
Interakce a charakterizace biomolekul
Analytical ultracentrifugation Analytical ultracentrifugation
CF: Core Facility Biomolecular Interaction and Crystalization
Automated calorimetric system Auto-iTC200 Automated calorimetric system Auto-iTC200
CF: Core Facility Biomolecular Interaction and Crystalization
Circular dichroism spectroscopy Circular dichroism spectroscopy
CF: Core Facility Biomolecular Interaction and Crystalization
Differential scanning calorimeter VP-DSC Differential scanning calorimeter VP-DSC
CF: Core Facility Biomolecular Interaction and Crystalization
Differential scanning fluorimetry - NanoTemper Prometheus Differential scanning fluorimetry - NanoTemper Prometheus
CF: Core Facility Biomolecular Interaction and Crystalization
Dynamic light scattering Dynamic light scattering
CF: Core Facility Biomolecular Interaction and Crystalization
Isothermal titration calorimetry VP-ITC Isothermal titration calorimetry VP-ITC
CF: Core Facility Biomolecular Interaction and Crystalization
Microdeposition system for biosensor arrays Microdeposition system for biosensor arrays
CF: Core Facility Biomolecular Interaction and Crystalization
Microscale Thermophoresis - NanoTemper Monolith Microscale Thermophoresis - NanoTemper Monolith
CF: Core Facility Biomolecular Interaction and Crystalization
Multichannel SPR system Multichannel SPR system
CF: Core Facility Biomolecular Interaction and Crystalization
SPR biosensor BiaCore T200 SPR biosensor BiaCore T200
CF: Core Facility Biomolecular Interaction and Crystalization
Krystalizace biomolekul
Automated storage and visual inspection of crystal plates (20 ° C) Automated storage and visual inspection of crystal plates (20 ° C)
CF: Core Facility Biomolecular Interaction and Crystalization
Automated storage and visual inspection of crystal plates (4 ° C) Automated storage and visual inspection of crystal plates (4 ° C)
CF: Core Facility Biomolecular Interaction and Crystalization
Gradient incubator for optimizing protein crystallization temperature Gradient incubator for optimizing protein crystallization temperature
CF: Core Facility Biomolecular Interaction and Crystalization
Robotics for protein crystallization Robotics for protein crystallization
CF: Core Facility Biomolecular Interaction and Crystalization
Seznam služeb
Biomolecular characterization and interaction
Calorimetric titration + automated software data evaluation. Calorimetric titration + automated software data evaluation. Calorimetric measurement of receptor-ligand interaction (Standard titration method, Single injection method) Data evaluation - by automated software data evaluation - complete thermodynamic profile determination (association constant, enthalpy, entropy, stoichiometry value) using curve fitting models: One set of binding site

Booking of the service is available via CEITEC intranet system
Calorimetric titration + expert data evaluation + data evaluation training AutoITC200 Calorimetric measurement of receptor-ligand interaction (Standard titration method, Single injection method) Data evaluation - manually by expert - complete thermodynamic profile determination (association constant, enthalpy, entropy, stoichiometry value) using curve fitting models: One set of binding site, Two sets of binding sites, Sequential Binding model. Determination of kinetic parameters Km and kcat. Data evaluation training.

Booking of the service is available via CEITEC intranet system
Calorimetric titration + expert data evaluation Calorimetric measurement of receptor-ligand interaction (Standard titration method, Single injection method) Data evaluation - manually by expert - complete thermodynamic profile determination (association constant, enthalpy, entropy, stoichiometry value) using curve fitting models: One set of binding site, Two sets of binding sites, Sequential Binding model. Determination of kinetic parameters Km and kcat.

Booking of the service is available via CEITEC intranet system
Microdeposition system for biosensor arrays - advanced optimization service Microdeposition system for biosensor arrays - advanced optimization service Compact automated non-contact dispensing system of ultra-low volumes of biomolecules and bioreagens. Advanced service involves advanced optimization of instrument settings in case of more complex and viscous samples and reagens.

Booking of the service is available via CEITEC intranet system
Sedimentation velocity Sedimentation velocity Sedimentation velocity method can be used for determination of sample dispersity, oligomeric state of proteins, the shape of the particle and it is also suitable for analysis of aggregates and a study of biomolecular interactions.

Booking of the service is available via CEITEC intranet system
Sedimentation equilibrium Sedimentation equilibrium Sedimentation equilibrium method can be used for accurate determination of molecular weights of various biomolecules and the study of their interactions.

Booking of the service is available via CEITEC intranet system
Microdeposition system for biosensor arrays - standard service Microdeposition system for biosensor arrays - standard service Compact automated non-contact dispensing system of ultra-low volumes of biomolecules and bioreagens.

Booking of the service is available via CEITEC intranet system
Crystallization of biomolecules
Standard crystallization screen set-up Standard crystallization screen set-up Set-up of crystallization screens (drop volume 200-300 nl) using commercial kits (including kits for membrane proteins, protein complexes and nucleic acids) - Sitting drop crystallization method, Crystallization under oil

Booking of the service is available via CEITEC intranet system
Customized crystallization Customized crystallization Setting-up multidimensional gradients for optimization (from up to 5 different solutions). Set-up of optimization screens - Hanging drop crystallization method, Sitting drop crystallization method, Crystallization under oil.

Booking of the service is available via CEITEC intranet system
Advanced crystallization techniques Advanced crystallization techniques Optimization of protein crystal production in large scale (manual setting) - Membrane protein crystallization techniques, Crystallization by dialysis or using capilaries Note: Service price is calculated individually. Contact the responsible person for details.

Booking of the service is available via CEITEC intranet system
Customized crystallization, Plate storage and inspection Customized crystallization, Plate storage and inspection Setting-up multidimensional gradients for optimization (from up to 5 different solutions). Set-up of optimization screens - Hanging drop crystallization method, Sitting drop crystallization method, Crystallization under oil. Storage of the screening plates for 3 months at a constant temperature 4°C or 20°C. Automatic screening of crystals - Regular automatic inspection within the period of one month, UV imaging to distinguish a protein from a salt. Online access to the images 24/7 Storage of the screening plates for extended period of time (6 months) at a constant temperature 4°C or 20°C with a possibility of a demanded extra inspection.

Booking of the service is available via CEITEC intranet system
Standard crystallization Screen Set-up, Plate Storage and Inspection Standard crystallization Screen Set-up, Plate Storage and Inspection Set-up of crystallization screens (drop volume 200-300 nl) using commercial kits (including kits for membrane proteins, protein complexes and nucleic acids). Sitting drop crystallization method, crystallization under oil. } Storage of the screening plates for 3 months at a constant temperature 4°C or 20°C Automatic screening of crystals . Regular automatic inspection within the period of one month. UV imaging to distinguish a protein from a salt. Online access to the images. Storage of the screening plates for extended period of time (6 months) at a constant temperature 4°C or 20°C with a possibility of a demanded extra inspection

Booking of the service is available via CEITEC intranet system
Plate storage and inspection Plate storage and inspection Storage of the screening plates for 3 months at a constant temperature 4°C or 20°C. Automatic screening of crystals. Regular automatic inspection within the period of one month. UV imaging to distinguish a protein from a salt. Online access to the images 24/7. Storage of the screening plates for extended period of time (6 months) at a constant temperature 4°C or 20°C with a possibility of a demanded extra inspection.

Booking of the service is available via CEITEC intranet system
Others
Consulting - assistance Service includes consulting with specialist, expert data evaluation, advanced experimental design or personal user support during measurement.

Booking of the service is available via CEITEC intranet system
Initial training for instruments in user mode (operated by users him-herself) Initial training for instruments which are operated by users him/herself. This includes Biacore T200 (SPR), multichannel SPR imaging system, DelsaMax Core (DLS), Jasco J-815 (CD), VP-ITC, VP-DSC, Monolith NT.115 Nano (MST), Prometheus (DSF), microdeposition system for biosensor arrays and gradient incubator for optimizing protein crystallization temperature. Training is performed by CF: BIC staff - responsible person for each instrument. Without this training users cannot operated the instruments on their own.

Booking of the service is available via CEITEC intranet system
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