2nd LINXS Symposium on Integrative Structural Biology

ID : 26 LP3 and DEMAX Content LP3 and DEMAX Wolfgang Knecht, Claes von Wachenfeldt and Zoe Fisher* Lund Protein Production Platform (LP3), Lund University, Sölvegatan 35, 223 62 Lund, Sweden and *Scientific Activities Division, European Spallation Source ERIC (ESS), Tunavägen 24, 221 00 Lund, Sweden. Proteins are diverse molecules and of enormous importance to life on earth. They have a multitude of different functions in all organisms and can work as enzymes, gene regulators, structural components, transporters, and receptors. In disease, most drugs act on proteins. It is therefore expected that the structures and mechanisms of proteins are prominent topics in life science research. Access to both state-of-the-art X-ray (MAX IV) and neutron sources (ESS) will increase the capacity for innovation in the life sciences. To enable efficient use of these unique and powerful facilities by Lund researchers, Lund University hosts the protein production platform, LP3 (www.lu.se/lp3). LP3 assists users with: 1) Recombinant protein production, 2) biophysical protein characterisation 3) High-throughput crystallization and structure determination, and 4) Stable isotope labelling and bio-deuteration of biological macromolecules. Since 2016, the DEuteration and MAcromolecular Xtallization (DEMAX) platform of the European Spallation Source ERIC (ESS) is co-localized with LP3. DEMAX and LP3 are coordinating in their efforts(1-4) to develop cost-effective production of deuterated proteins for macromolecular crystallography, enable crystallization of interesting proteins for neutron work, and for the production of labelled proteins/lipids for neutron reflectometry. For more information and access see: www.lu. se/lp3 1 Koruza, K. , Lafumat, B. , Nyblom, M. , Knecht, W. & Fisher, Z. From initial hit to crystal optimization with microseeding of human Carbonic anhydrase IX—A case study for neutron protein crystallography. Crystals 8, 434 (2018). 2 Koruza, K. , Lafumat, B. , Vegvari, A. , Knecht, W. & Fisher, S. Z. Deuteration of human carbonic anhydrase for neutron crystallography: Cell culture media, protein thermostability, and crystallization behavior. Archives of biochemistry and biophysics 645, 26-33, doi:10.1016/j.abb. 2018.03. 008 (2018). 3 Koruza, K. , Mahon, B.P., Blakeley, M.P., Ostermann, A. , Schrader, T.E. , McKenna, R. , Knecht, W. , Fisher, SZ. Using neutron crystallography to elucidate the basis of selective inhibition of carbonic anhydrase by saccharin and a derivative. Journal of structural biology 205, 147-154, doi:10.1016/j.jsb. 2018.12. 009 (2019). 4 Kelpsas, V. , Lafumat, B. , Blakeley, M.P., Coquelle, N. , Oksanen, E. & von Wachenfeldt, C. Perdeuteration, large crystal growth and neutron data collection of Leishmania mexicana triose-phosphate isomerase E65Q variant Acta Cryst. F 75, 260-269, doi: 10.1107/S2053230X19001882 (2019) Primary author(s) : KNECHT, Wolfgang (Lund University); FISHER, Zoe; VON WACHENFELDT, Claes Presenter(s) : KNECHT, Wolfgang (Lund University) Submitted by KNECHT, Wolfgang on Tuesday 04 June 2019 2nd LINXS Symp . / Report of Abstracts Structural transitions in protein.