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An international collaboration between the Lund Protein Production Platform (LP3), the UCL School of Pharmacy and ESS, through its DEMAX platform, has initiated biophysical and structural studies of three non-structural proteins from the novel coronavirus, SARS CoV-2, the causative agent of COVID-19. Recently we managed to solve the structure of one of these proteins, Nsp10, by using the BioMAX be

https://www.lp3.lu.se/article/collaborative-research-project-corona-virus-proteins - 2025-11-19

Results from the collaborative corona virus protein research project involvning Lund Protein Production Platform (LP3), the UCL School of Pharmacy and ESS, through its DEMAX platform have been published in the International Journal of Molecular Sciences.

https://www.lp3.lu.se/article/results-collaborative-corona-virus-protein-research-project-published - 2025-11-19

LP3 activities will be limited during the summer, especially in July and early August. In the meantime, here’s some recommended summer reading:

https://www.lp3.lu.se/article/recommended-summer-reading - 2025-11-19

FragMAX, a project run in collaboration between LP3, MAXIV, Astra Zeneca and SARomics Biostructures, has been awarded funding from the Swedish Research Council. The project aims to establish a fragment based screening facility, enabling scientists and small companies to screen low molecular weight fragments for binding to target proteins using X-ray crystallography.Read more about the FragMAX proj

https://www.lp3.lu.se/article/fragmax-awarded-funding-swedish-research-council - 2025-11-19

LP3 was successful in its application for renewal of beamtime access at BioMAX (the X-ray macromolecular crystallography beamline of MAX IV). The protein structure pipeline at LP3 is now established. Users can get their protein samples crystallised and the resulting crystals can on a regular basis be evaluated for diffraction and data can be collected. Processing of X-ray data and solving structur

https://www.lp3.lu.se/article/renewal-beamtime-access-biomax-and-allocated-time-scilifelab-cryo-em-facility - 2025-11-19

A team from the Lund Protein Production Platform, Karolinska Institute, and the European Spallation Source have published an optimised approach to high-yield protein deuteration at low cost, for neutron protein crystallography in Archives of Biochemistry and Biophysics (external website). 

https://www.lp3.lu.se/article/more-less-low-cost-high-yield-protein-deuteration-neutron-crystallography - 2025-11-19

The baculovirus-insect cell expression system has become one of the most widely used eukaryotic expression systems for heterologous protein production in many laboratories. To date, limited data has been presented in the literature to benchmark the protocols used for baculovirus vectors, and this study facilitates the selection of a system for optimal production of target proteins. The benchmarkin

https://www.lp3.lu.se/article/baculovirus-driven-protein-expression-insect-cells-benchmarking-study - 2025-11-19

LP3 has been granted beamtime at the X-ray macromolecular crystallography beamline of MAX IV, BioMAX. This allows users to have their crystals rapidly evaluated for diffraction. With funding from BioCARE (a governmental supported strategic research area in cancer (external website)) the Lund Protein Production Platform, LP3, can also offer the possibility to process data and solve structures. Assi

https://www.lp3.lu.se/article/beamtime-biomax - 2025-11-19

The Lund Protein Production Platform is one of several protein production facilities in Sweden that form the Protein Production Network Sweden (PPNS), each with its own specialties and focus. PPNS is an informal network formed in 2013 between protein production facilities at Swedish universities. The overall aim is to make competence and protein production methodologies available to the Swedish ac

https://www.lp3.lu.se/article/protein-production-network-sweden-launches-new-website - 2025-11-19

The DEuteration and MAcromolecular Xtallisation (DEMAX) platform of the European Spallation Source ERIC (ESS) moved into Biology House A at Lund University and is now co-localised with the Lund Protein Production Platform (LP3). DEMAX (external website) and LP3 are collaborating to coordinate their efforts to develop cost-effective production of deuterated biomaterials (lipids and proteins) for ne

https://www.lp3.lu.se/article/partnership-between-lp3-and-demax - 2025-11-19

A Bioscreen C system for microbiological growth studies is now available at LP3. The Bioscreen C (external website) can incubate, shake, and measure the turbidity (OD) of up to 200 samples simultaneously. 

https://www.lp3.lu.se/article/new-system-microbiological-growth-monitoring - 2025-11-19

LP3 is part of the Protein Production Network Sweden (PPNS) that aims to make multiple protein expression hosts, methodologies and competence in protein production available to the Swedish academic life science community. Collaboration between Swedish protein production sites is crucial in order to solve complex scientific questions and in a pilot effort to test a new joint approach, five proteins

https://www.lp3.lu.se/article/protein-production-network-sweden-pilot-expression-screen-completed - 2025-11-19

LP3 is taking part in the formation of a network of Swedish protein production facilities together with Protein Science Facility at Karolinska Institutet/SciLifeLab (external website) Mammalian Protein Expression at Göteborg University (external website) Protein Expertise Platform at Umeå University (external website) Drug Discovery and Development platform at SciLifeLab (external website) The net

https://www.lp3.lu.se/article/network-swedish-protein-production-facilities - 2025-11-19

Right now LP3 is in the process of establishing the Baculovirus Expression Vector System (BEVS) – a system for expression of recombinant proteins in insect cells. This system will complement the current LP3 capabilities to express proteins in bacteria and yeast. The BEVS, being a eukaryotic expression system, has its strength in producing proteins from higher eukaryotic organisms that have failed

https://www.lp3.lu.se/article/eukaryotic-expression-system - 2025-11-19

Under den pågående CoViD-19 pandemin har förståelsen för virusets proteiner varit en central del i forskningen om SARS-CoV-2, eftersom det är genom proteinkontakter som viruset invaderar människans celler. På flera universitet i Sverige finns faciliteter som producerar proteiner för olika forskningsprojekt och som ingår i ett nätverk kallat Protein Produktion Sverige (PPS). PPS har genom sitt nati

https://www.lp3.lu.se/article/med-proteiner-som-nycklar-till-sars-cov-2-sa-har-vi-lart-oss-mer-om-viruset - 2025-11-19

By fragment screening using x-ray crystallography we identified four ligands revealing ligand-binding sites in conserved interfaces between SARS-CoV-2 nsp10 and nsp14/nsp16. The nsp14/10 interaction is weak and therefore could be disrupted by small molecules. In a collaborative effort, the Lund Protein Production Platform (LP3), the FragMAX platform at the BioMAX beamline of the MAX IV laboratory,

https://www.lp3.lu.se/article/fragmax-library-identifies-ligand-binding-sites-nsp10-and-nsp1416-interfaces-sars-cov-2 - 2025-11-19

The new protein production platform will start in the beginning 2022 and is a co-operation between five Swedish universities. A new nationally distributed infrastructure - Protein Production Sweden or Proteinproduktion Sverige (PPS) in Swedish, will start up in the beginning of 2022. This is made possible thanks to a five-year-grant (until 2026) from the Swedish Research Council. Together, five un

https://www.lp3.lu.se/article/new-national-infrastructure-protein-production-sweden-pps - 2025-11-19

LP3 extends its portfolio of machines available for biophysical analysis by welcoming the OMNISEC system from Malvern Panalytical. Thanks to a grant from Olle Engkvisits foundation to Prof. Anders Malmström (Experimental Medical Sciences, Lund University), we now host a state of the art multi-detection size exclusion chromatography (SEC) system: OMNISEC. The OMNISEC system is now available to user

https://www.lp3.lu.se/article/now-lp3-absolute-molecular-weight-determination-proteins - 2025-11-19

Wolfgang Knecht, head of LP3 presented the capabilities of LP3 in biophysics and protein structure determination at the first Swedish national PI-meeting in Biochemistry, Biophysics and Molecular Biology (external webpage). The meeting was jointly organized by the Swedish Society for Biochemistry, Biophysics and Molecular Biology, SFBBM(external webpage, in Swedish) and the Swedish National Commit

https://www.lp3.lu.se/article/lp3-presented-swedish-national-pi-meeting-biochemistry-biophysics-and-molecular-biology - 2025-11-19

To strengthen the engagement of the Swedish scientific community in ESS, Sweden has now officially become part of the ESS in-kind community with four projects selected by ESS and the Swedish Research Council. To strengthen the engagement of the Swedish scientific community in the European Spallation Source (ESS), Sweden has now officially become part of the ESS in-kind community with a number of c

https://www.lp3.lu.se/article/sweden-enters-kind-agreement-ess-lp3-contributes-deuteration-lab-services - 2025-11-19