Membrane-protein crystals for neutron diffraction

Thomas Lykke Møller Sørensen, Samuel John Hjorth-Jensen, Esko Oksanen, Jacob Lauwring Andersen, Claus Olesen, Jesper Vuust Møller, Poul Nissen

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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.

Original languageEnglish
JournalActa crystallographica Section D: Structural biology
IssuePt 12
Pages (from-to)1208-1218
Number of pages11
Publication statusPublished - 1 Dec 2018


  • SERCA1
  • membrane-protein crystallization
  • neutron macromolecular crystallography
  • structural biology


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