Protein crystallography lab.

Facility manager: Dr. Veronika Harmat

Members: Zsolt Dürvanger, Dániel Forray, Dr. Veronika Harmat, Gergő Hegedűs, Dr. Dóra K. Menyhárd , Anna Kiss-Szemán, Máté Sulyok-Eiler

For a better understanding of function and interactions of biological macromolecules, 3D-structure is required at an atomic resolution, typically determined by protein crystallography; a perfect method of choice. On the other hand, small molecular crystallographic studies explore the structural basis of physical-chemical characteristics of the compound. In 2018. new X-ray crystallographic instruments were installed in the EU 2020 framework (Széchenyi 2020*). The aim of these consortial projects is to establish an infrastructure serving as an open lab for a wider range of research groups (ELTE-CrystalLAB). The Rigaku XtaLAB Synergy-R X-ray diffractometer is capable for small molecular and protein crystallographic data collection as well as in situ crystal testing. A TTP Labtech Mosquito-LCP is available for automated crystallization, and monitoring crystal growth is carried out by a Formulatrix Rock Imager 2 system.

*The research within project No. VEKOP-2.3.3-15-2017-00018 and VEKOP-2-3-2-16-2017-00014 was supported by the European Union and the State of Hungary, co-financed by the European Regional Development Fund.

Laboratory News

  • X-Ray diffraction data collection at synchrotron sources

    We visited European microfocus synchrotron sources at ESRF and BESSY.


  • Scientific meeting at the Hungarian Academy of Sciences on the occasion of the International Year of Crystallography

    We participated at the scientific meeting organised by the Sections of the Physical, Chemical and Biological Sciences of the Hungarian Academy of Sciences on the occasion of the International Year of Crystallography 2014. We presented the story of discovering structure/function relationships of enzymes of the prolyl oligopeptidase family

    Iycr Square 190x182


  • Veronika Harmat , Klarissza Domokos , Dóra K. Menyhárd , Anna Palló , Zoltán Szeltner , Ilona Szamosi , Tamás Beke , Gábor Náray-Szabó , László Polgár
    Structure and catalysis of acylamonoacyl peptidase: closed and open subunits of a dimer oligopeptidase
    Journal of Biological Chemistry 286:1987-1998. PMID: 21084296 | DOI: 10.1074/jbc.M110.169862 (2011) Kivonat
  • József Dobó , Veronika Harmat , László Beinrohr , Edina Sebestyén , Péter Závodszky , Péter Gál
    MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity
    J. Immunol. 183:1207-1214. (2009) Kivonat
  • László Beinrohr , Veronika Harmat , József Dobó , Zsolt Lörincz , Péter Gál , Péter Závodszky
    C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease
    J. Biol. Chem. 282: 21100-21109. (2007) Kivonat
  • Márton Megyeri , Veronika Harmat , Balázs Major , Ádám Végh , Júlia Balczer , Dávid Héja , Katalin Szilágyi , Dániel Datz , Gábor Pál , Péter Závodszky , Péter Gál , József Dobó
    Quantitative characterization of the activation steps of Mannan-Binding Lectin (MBL)-Associated Serine Proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway
    J Biol Chem 288(13):8922-8934. | DOI: 10.1074/jbc.M112.446500 | PMID: 23386610 (2013) Kivonat
  • Dóra K. Menyhárd , Anna Kiss-Szemán , Éva Tichy-Rács , Balázs Hornung , Krisztina Rádi , Zoltán Szeltner , Klarissza Domokos , Ilona Szamosi , Gábor Náray-Szabó , László Polgár , Veronika Harmat
    A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization
    J Biol Chem 288(24):17884-17894. | DOI: 10.1074/jbc.M113.451534 | PMID: 23632025 (2013) Kivonat