Protein crystallography lab.
Facility manager: Dr. Veronika Harmat
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.
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
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
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