Membrane-protein crystals for neutron diffraction

Research output: Contribution to journalReview article


Neutron macromolecular crystallography (NMX) has the potential to provide the experimental input to address unresolved aspects of transport mechanisms and protonation in membrane proteins. However, despite this clear scientific motivation, the practical challenges of obtaining crystals that are large enough to make NMX feasible have so far been prohibitive. Here, the potential impact on feasibility of a more powerful neutron source is reviewed and a strategy for obtaining larger crystals is formulated, exemplified by the calcium-transporting ATPase SERCA1. The challenges encountered at the various steps in the process from crystal nucleation and growth to crystal mounting are explored, and it is demonstrated that NMX-compatible membrane-protein crystals can indeed be obtained.


  • Thomas Lykke Møller Sørensen
  • Samuel John Hjorth-Jensen
  • Esko Oksanen
  • Jacob Lauwring Andersen
  • Claus Olesen
  • Jesper Vuust Møller
  • Poul Nissen
External organisations
  • Aarhus University
  • European Spallation Source ESS AB
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Structural Biology


  • membrane-protein crystallization, neutron macromolecular crystallography, SERCA1, structural biology
Original languageEnglish
Pages (from-to)1208-1218
Number of pages11
JournalActa Crystallographica Section D: Structural Biology
Issue number12
Publication statusPublished - 2018 Dec
Publication categoryResearch