Lund Protein Production Platform and Lund University Node of Protein Production Sweden


  • Location


Infrastructure Details



Name of national/international infrastructure this infrastructure belongs to

• Protein Production Sweden (PPS)
• The European association Core Technologies for the Life Sciences
• The P4EU (Protein Production and Purification Partnership in Europe)
• The EATRIS, the European infrastructure for translational medicine and EATRIS small molecule platform
• The European Deuteration Network DEUNET
• FragMAX – a facility for high throughput fragment screening in drug development by X-ray crystallography
• The DEuteration and MAcromolecular Xtallization (DEMAX) platform of the European Spallation Source ERIC (ESS) (collaboration)


Lund Protein Production Platform, LP3, is a cross-faculty facility for protein production, purification and crystallisation, primarily directed at academic research groups based at Lund University. LP3 is also Lund Universities node of the Protein Production Sweden (PPS)

Equipment and resources

LP3 is fully equipped for recombinant protein production in E. coli and insect cells (BEVS) and protein purification using state of the art chromatography systems.

• Equipment for SDS-PAGE, Western blotting and other standard equipment for protein characterisation.
• Biophysical characterisation with differential scanning fluorimetry (DSF) and dynamic light scattering (DSL).
• Enzymatic activity assays.
• Electronic laboratory notebooks are used for documentation.

For crystallisation, the facility is equipped with state-of-the-art nanolitre pipetting equipment with capability to handle lipidic cubic phases for membrane proteins, as well as a plate hotel with the capacity to store and automatically image up to 256 plates, each with up to 288 crystallization trials. A Tecan liquid handling system and a Dragonfly liquid handler for the preparation of focused crystallisation screens are also available. For optimisation of seeding conditions we have access to an Oryx8.

LP3 is colocalised with and closely collaborates with the DEMAX platform of the ESS on production of deuterium labeled biomolecules (proteins, lipids) for neutron scattering experiments and the development of methods for crystal growth for neutron crystallography.

LP3 is the only academic protein production platform in Sweden providing specialisation in protein production using the baculovirus expression vector system (BEVS, insect cells) and perdeuteration of biological macromolecules.

LP3 has regular access to regular beamtime at BioMAX, the X-ray macromolecular crystallography beamline of MAX IV), for testing crystals produced at LP3 and to collect datasets. LP3 can further process data, solve and refine protein structures.

LP3 is a unique entry point and partner for both research aiming at conventional x-ray protein structure determination, as well as for enabling research using neutron scattering techniques that require deuterated bioreagents.

Services provided

LP3 offers services for the entire process chain of production, purification, characterization, protein crystallisation and protein structure determination and structure refinement, or each individual step in the chain:

• Plasmids for protein production
• Microbiological growth monitoring (Bioscreen C)
• Recombinant protein production in bacterial (E. coli) or eukaryotic (insect) cells.
• Protein labeling (seleno-methionine incorporation, labeling with stable isotopes
   (2H, 13C, 15N), biotinylation, phosphorylation)
• Protein purification
• Biophysical protein characterization by Size Exclusion Chromatography (SEC),
   Dynamic Light Scattering (DLS) and Differential Scanning Fluorimetry (DSF)
• High-throughput & nanovolume protein crystallization
• Automated crystallization plate storage and imaging
• Protein structure determination and refinement:
• Application for beamtime (LP3 has regular beamtime at BioMAX, the X-ray
   macromolecular crystallography beamline of MAX IV).
• MX data collection at synchrotron beamline (BioMAX MAX IV)
• Process x-ray data and determine and refine the structures
• Cryo-EM screening, LP3 is part of a BAG for Cryo-EM in Stockholm

Management of the infrastructure

LP3 is governed by a board of one chairman and six members, one each from Faculty of Science, Faculty of Medicine, Faculty of Technology, MAX IV and the European Spallation Source (ESS) (external member) and one student. The chairman is the dean or vice dean of the Faculty of Science. The daily business of the center is led by a manager (Dr. Wolfgang Knecht).

LP3 is located at the Biology Department (Biology Building A, Sölvegatan 35, 22362 Lund), within the Faculty of Science at LundUuniversity. LP3 is a separate entity within the existing administrative structure of the Department of Biology and follows the working and delegation principles of the Faculty of Science.
Photo associated with equipment

UKÄ subject classification

  • Medical and Health Sciences
  • Engineering and Technology
  • Natural Sciences
  • Agricultural Sciences
  • Agricultural Biotechnology
  • Other Chemical Engineering
  • Pharmaceutical Chemistry
  • Bio Materials
  • Biocatalysis and Enzyme Technology
  • Bioprocess Technology
  • Medical Biotechnology
  • Other Industrial Biotechnology
  • Pharmaceutical Biotechnology
  • Cell and Molecular Biology
  • Medicinal Chemistry
  • Other Basic Medicine
  • Other Medical Biotechnology
  • Biomaterials Science
  • Biological Sciences
  • Chemical Sciences
  • Other Natural Sciences
  • Biochemistry and Molecular Biology
  • Biophysics
  • Structural Biology
  • Other Chemistry Topics

Type of infrastructure

  • Equipment
  • Services


  • Protein Production
  • Structural Biology
  • Protein Structure
  • Stable isotope labeling
  • Deuteration
  • Biophysics
  • Baculovirus vector expression system ( BEVS )
  • Fragment screening
  • Crystallography
  • Protein Purification
  • Protein Expression
  • Neutron
  • Neutron scattering
  • DSL
  • DSF

Infrastructure programme

  • Has current status as Infrastructure of national interest (Swedish Research Council)