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Centrální laboratoř RTG difrakce a Bio-SAXS

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Head of Core Facility
Researcher ID
Telefon: +420 54949 7576, +420 54949 5740
E-mail: ,
Kancelář:

Main Activity

X-ray Diffraction and Bio-SAXS core facility is equipped with top-class instruments for diffraction experiments with single crystal samples focused on the determination of the 3-D structure of (macro) molecules down to atomic resolution and for small angle X-ray scattering (SAXS) experiments with isotropically scattering samples focused on determination of the shape and size of macromolecules or nanoparticles. 

The range of applicable molecular mass for diffraction methods: from 100 up to 1000000, where the lower value covers molecules significant for nanotechnology, materials science or pharmacology and the upper limit covers biomacromolecules such as nucleic acids, proteins and their complexes. 

Range of applicable particle sizes for SAXS: from 2 to 100 nm.

Unique Features

  • The diffraction of X-rays in single crystal samples is the most important and – if an appropriate sample is available – also the fastest methodology currently available for the determination of the atomic structures of molecules and/or macromolecules and their complexes.

  • On the other hand, SAXS is a technique capable of determining structural characteristics such as mono dispersity or aggregation, oligomeric state, low resolution three-dimensional shape or even quaternary structure not from a crystal but from a solution of (bio) macromolecules.

  • The centralized organization of expensive instrumentation for SAXS and single crystal studies and highly trained staff allow the cost-effective use of resources and obtaining of experimental results in rapid responses to the demands of even untrained users.

Key Equipment (Core Facility fully operational from 2014)

  • Rigaku HighFlux HomeLab™ robotized macromolecular diffraction system with ACTOR sample changer optimized for work at Cu-Kα wavelength

  • Rigaku HighFlux HomeLab™ universal, dual wavelength (Mo-Kα and Cu-Kα) diffractometer

  • Rigaku BioSAXS-1000 SAXS camera for small angle X-ray scattering from solutions of biological macromolecules

rigaku
Rigaku BioSAXS-1000

The Core Facility is part of Czech National Affiliated Centre of INSTRUCT. 

All CEITEC core facilities are available to external users (academia and companies). Czech and international researchers from universities and research institutes interested in accessing core facilities can benefit from support of research infrastructure CIISB, funded by the Ministry of Education, Youth and Sports of the Czech Republic.

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seznam / vizitky

Jméno a pozice

E-mail

Telefon

Mgr. Tomáš Klumpler, Ph.D.
Výzkumný pracovník - postdoc
+420 54949 7576, +420 54949 3430
doc. RNDr. Jaromír Marek, Ph.D.
Výzkumný pracovník
+420 54949 7576, +420 54949 5740
Bc. Gabriela Jalová
Organizační referent
+420 54949 1454

VYBRANÉ PUBLIKACE

2017

  • FIALA, T; LUDVIKOVA, L; HEGER, D; SVEC, J; SLANINA, T; VETRAKOVA, L; BABIAK, M; NECAS, M; KULHANEK, P; KLAN, P; SINDELAR, V, 2017:Bambusuril as a One-Electron Donor for Photoinduced Electron Transfer to Methyl Viologen in Mixed Crystals. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 139 (7), p. 2597 - 2603.
  • JASNOVIDOVA, O; KLUMPLER, T; KUBICEK, K; KALYNYCH, S; PLEVKA, P; STEFL, R, 2017:Structure and dynamics of the RNAPII CTDsome with Rtt103. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 114 (42), p. 11133 - 11138.

2015

  • DRUSAN, M; RAKOVSKY, E; MAREK, J; SEBESTA, R, 2015:Asymmetric One-Pot Conjugate Addition of Grignard Reagents to alpha,beta-Unsaturated Compounds Followed by Reaction with Carbenium Ions. ADVANCED SYNTHESIS & CATALYSIS 357 (7), p. 1493 - 1498.
  • STYSKALIK, A; SKODA, D; MORAVEC, Z; BABIAK, M; BARNES, CE; PINKAS, J, 2015:Control of micro/mesoporosity in non-hydrolytic hybrid silicophosphate xerogels. JOURNAL OF MATERIALS CHEMISTRY A 3 (14), p. 7477 - 7487.

2011

  • HUDSON, JJR; BEDNAROVA, K; KOZAKOVA, L; LIAO, CY; GUERINEAU, M; COLNAGHI, R; VIDOT, S; MAREK, J; BATHULA, SR; LEHMANN, AR; PALECEK, J, 2011:Interactions between the Nse3 and Nse4 Components of the SMC5-6 Complex Identify Evolutionarily Conserved Interactions between MAGE and EID Families. PLOS ONE 6 (2)
  • PEKAROVA, B; KLUMPLER, T; TRISKOVA, O; HORAK, J; JANSEN, S; DOPITOVA, R; BORKOVCOVA, P; PAPOUSKOVA, V; NEJEDLA, E; SKLENAR, V; MAREK, J; ZIDEK, L; HEJATKO, J; JANDA, L, 2011:Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana. PLANT JOURNAL 67 (5), p. 827 - 839.

PROJEKTY

  • CIISB - České centrum pro integrativní strukturní biologii (LM2015043), MEYS, 2016 - 2019
  • CIISB4HEALTH - Česká infrastruktura pro integrativní strukturní biologii pro lidské zdraví (CZ.02.1.01/0.0/0.0/16_013/0001776), MEYS, 2017 - 2021
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Equipment Research group / CF Profile card
Liquid nitrogen Dewar for crystal transport and storage CF: Core Facility X-Ray Diffraction and Bio-SAXS
Rigaku BioSAXS-1000 SAXS camera for small angle X-ray scattering from solutions of biological macromolecules Rigaku BioSAXS-1000 SAXS camera for small angle X-ray scattering from solutions of biological macromolecules
CF: Core Facility X-Ray Diffraction and Bio-SAXS
Rigaku HighFlux HomeLab™ universal, dual wavelength (Mo-K_α and Cu-K_α ) diffractometer Rigaku HighFlux HomeLab™ universal, dual wavelength (Mo-K_α and Cu-K_α ) diffractometer
CF: Core Facility X-Ray Diffraction and Bio-SAXS
Rigaku HighFlux HomeLab™ robotized macromolecular diffraction system with ACTOR sample changer optimized for work at Cu-K_α wavelength Rigaku HighFlux HomeLab™ robotized macromolecular diffraction system with ACTOR sample changer optimized for work at Cu-K_α wavelength
CF: Core Facility X-Ray Diffraction and Bio-SAXS

 

  • Quality control of solution of biological macromolecules prior crystallization and/or SAXS
  • Basic characterization of solutions of biological macromolecules by SAXS
  • Determination of a low resolution 3-D shape of biological macromolecules by SAXS
  • SAXS characterization of nanoparticles
  • Robotized high throughput initial screening of crystallization conditions for biomacromolecules
  • Optimization of selected crystallization conditions
  • Screening and optimization of conditions for cryoprotection of protein crystals
  • Testing of the diffraction quality of protein crystals, derivatives, etc. prior to data collection
  • Collection of diffraction data from crystals of biological macromolecules at home source
  • Data collection and solving of crystal structures from non-biological single crystals

More complex services, training courses, access to a wide list of crystallisation instrumentation purchased within the past projects at Masaryk University and/or help with diffraction data analysis are available on request.

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