15–17 May 2017
Oxford Spires Hotel
Europe/Stockholm timezone

LP3 and DEMAX

Not scheduled
20m
Oxford Spires Hotel

Oxford Spires Hotel

Abingdon Rd Oxford OX1 4PS UK
Poster abstract Overview of Deuteration facilities

Description

Wolfgang Knecht (1) and Zoe Fisher (1,2) (1) Lund Protein Production Platform (LP3), Lund University, Sölvegatan 35, 22362 Lund, Sweden and (2) Scientific Activities Division, European Spallation Source ERIC (ESS), Tunavägen 24, 22100 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 unsurprising 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) High-throughput crystallization, and 3) Stable isotope labelling and bio-deuteration of biological macromolecules (proteins and lipids). In July 2016, the DEuteration and MAcromolecular Xtallization (DEMAX) platform of the European Spallation Source ERIC (ESS) moved into Biology House A at Lund University and co-localized with LP3. DEMAX and LP3 are coordinating in their efforts to develop cost-effective production of deuterated proteins for macromolecular crystallography, enable crystallization of interesting proteins for neutron work, and for the production of labeled proteins/lipids for neutron reflectometry. For more information and access see: www.lu.se/lp3

Primary authors

Dr Wolfgang Knecht (Lund University) Zoe Fisher (European Spallation Source ERIC)

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