Membrane-protein crystals for neutron diffraction

Forskningsoutput: TidskriftsbidragÖversiktsartikel

Abstract

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.

Detaljer

Författare
  • Thomas Lykke Møller Sørensen
  • Samuel John Hjorth-Jensen
  • Esko Oksanen
  • Jacob Lauwring Andersen
  • Claus Olesen
  • Jesper Vuust Møller
  • Poul Nissen
Enheter & grupper
Externa organisationer
  • Aarhus University
  • European Spallation Source ESS AB
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Strukturbiologi

Nyckelord

Originalspråkengelska
Sidor (från-till)1208-1218
Antal sidor11
TidskriftActa Crystallographica Section D: Structural Biology
Volym74
Utgåva nummer12
StatusPublished - 2018 dec
PublikationskategoriForskning
Peer review utfördJa