Infrastructure Details
Acronym
Name of national/international infrastructure this infrastructure belongs to
• 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)
Description
LP3 harbors the LU node of a new national research infrastructure for protein production: Protein Production Sweden (PPS, www.gu.se/pps) and is part of MAX IV FragMAX platform for X-ray aided fragment screening (https://www.maxiv.lu.se/fragmax/). In addition, LP3 provides the laboratories for the biological part of the Deuteration and Macromolecular Crystallization (DEMAX, https://europeanspallationsource.se/science-support-systems/demax) platform of the European Spallation Source ERIC (ESS) and closely collaborates with DEMAX. The service facility is integrated with research training and development of skills in experimental protein science for PhD students and postdocs.
Equipment and resources
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 hotels with the capacity to store and automatically image crystallisation plates. 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
For more information please see www.lu.se/lp3
Management of the infrastructure
For further informations about LP3 please see www.lu.se/lp3
For further informations about LP3 please see www.gu.se/pps
Subject classification (UKÄ)
- Medical and Health Sciences
- Engineering and Technology
- Natural Sciences
- Agricultural and Veterinary sciences
- Agricultural Biotechnology
- Other Chemical Engineering
- Bio Materials
- Biocatalysis and Enzyme Technology
- Bioprocess Technology (including Bioengineering Equipment)
- Pharmaceutical and Medical Biotechnology
- Other Industrial Biotechnology
- Cell and Molecular Biology
- Medicinal Chemistry
- Other Basic Medicine
- Other Medical Biotechnology
- Biomaterials Science
- Biological Sciences
- Chemical Sciences
- Other Natural Sciences
- Biophysics
- Structural Biology
- Other Chemistry Topics
Free keywords
- 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 category
- European Research Infrastructure Consortium (ERIC)
- Infrastructure of National Interest (Swedish Research Council)
- University Core Facility
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A truncated CDC14A retains catalytic structure and phosphatase activity preserving male fertility but causes nonsyndromic deafness
Shabbir, K., Jackisch, G., Belyantseva, I. A., Imran, M., Naz, S., Sele, C., Murina, V., Knecht, W., Friedman, T. B., Logan, D. T. & Imtiaz, A., 2026, In: The Journal of biological chemistry. 302, 1, 110982.Research output: Contribution to journal › Article › peer-review
Open Access -
A single residue affects the dynamics and shape of a tetrameric GH43 β-1,4-d-xylosidase from Levilactobacillus brevis DSM1269
Linares-Pastén, J. A., Faryar, R., Torrez Alvarez, S., Albasri, K., Shuoker, B., Abou Hachem, M., Logan, D. T. & Karlsson, E. N., 2025 Oct, In: Protein Science. 34, 10, p. e70299 19 p.Research output: Contribution to journal › Article › peer-review
Open Access -
Off-target binding of the histone deacetylase inhibitor vorinostat to carbonic anhydrase II and IX
Gulkis, M. C., Hodgkinson, J. T., Sele, C. P., Knecht, W., McKenna, R. & Fisher, S. Z., 2025 Sept 1, In: Acta Crystallographica Section F Structural Biology Communications. 81, 9, p. 388-397Research output: Contribution to journal › Article › peer-review
Open Access -
Structural basis for small molecule binding to the SARS-CoV-2 nsp10–nsp14 ExoN complex
Kozielski, F., Fisher, Z., Ma, S., Al Busaidi, F., Krupinska, E., Nyblom, M., Sele, C., McDuffie Sullivan, H., Krojer, T. & Knecht, W., 2025 Aug 5, In: Nucleic Acids Research. 53, 14, gkaf753.Research output: Contribution to journal › Article › peer-review
Open Access -
FragMAX Facility for Crystallographic Fragment and Ligand Screening at MAX IV
Kanchugal P., S., Jagudin, E., Lima, G. M. A., Talibov, V. O., Begum, A., Nan, J., Eguiraun, M., Gonzalez, A., Sele, C., Nyblom, M., Knecht, W., Logan, D. T., Sjögren, T., Thunnissen, M., Ursby, T., Obiols‐Rabasa, M., Larsson, M., Mueller, U. & Krojer, T., 2025 Feb 1, In: Applied Research. 4, 1, 11 p., e202400263.Research output: Contribution to journal › Article › peer-review
Open Access -
Deciphering protective immunity by multimodal mass spectrometry: Towards epitope-focused streptococcal vaccines
Tang, D., 2025, Lund: Lund University, Faculty of Medicine. 93 p.Research output: Thesis › Doctoral Thesis (compilation)
Open AccessFile418 Downloads (Pure) -
NK-A 17E-233I: a novel competitive inhibitor of human dihydroorotate dehydrogenase (DHODH) for cancer therapy
Anwar, M. M., Meseguer, S., García-Rodríguez, N., Krupinska, E., Sele, C., Rodríguez-Jiménez, A., Verma, S., Sagadevan, S., Ramon, J., Martí, R., Occhipinti, A., Angione, C., Ordóñez-Morán, P., Knecht, W., Huertas, P. & Juanes, M. A., 2025, In: Journal of Experimental & Clinical Cancer Research. 44, 292.Research output: Contribution to journal › Article › peer-review
Open Access
Projects
- 2 Finished
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HALOS: Hanseatic League of Science
Paulsson, K. M. (PI), Pearson, A. (CoI), Gajhede, M. (Researcher), Mårtensson, E. (CoI), Øster, J. (CoI), Thunnissen, M. (CoI), Oksanen, E. (CoI), Cardenas, M. (CoI), Bjorholm Dahl, A. (CoI), Rom Andersen, G. (CoI), Wilmanns, M. (CoI), Feidenhans'l, R. (CoI), Müller, N. (CoI), Lund, R. (CoI) & Gottwald, J. (CoI)
2019/02/01 → 2022/01/31
Project: Network
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FragMAX - a facility for high throughput fragment screening in drug development by X-ray crystallography
Lima, G. (Project coordinator), Müller, U. (Researcher), Knecht, W. (Researcher), Logan, D. (Researcher), Zawierucha, A. (Administrator), Sjögren, T. (Researcher), Talibov, V. (Researcher), Jagudin, E. (Researcher), Gourdon, M. (Researcher) & Sele, C. (Researcher)
2019/01/19 → 2022/01/18
Project: Research