Prospects for membrane protein crystals in NMX

Samuel John Hjorth-Jensen, Esko Oksanen, Poul Nissen, Thomas Lykke Møller Sørensen*

*Corresponding author for this work

Research output: Contribution to book/anthology/report/proceedingBook chapterResearchpeer-review

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Adding hydrogen atoms and protonation states to structures of membrane proteins requires successful implementation of neutron macromolecular crystallography (NMX). This information would significantly increase our fundamental understanding of the transport processes membrane proteins undertake. To grow the large crystals needed for NMX studies requires significant amounts of stable protein, but once that challenge is overcome there is no intrinsic property of membrane proteins preventing the growth of large crystals per se. The calcium-transporting P-type ATPase (SERCA) has been thoroughly characterized biochemically and structurally over decades. We have extended our crystallization efforts to assess the feasibility of growing SERCA crystals for NMX—exploring microdialysis and capillary counterdiffusion crystallization techniques as alternatives to the traditional vapor diffusion crystallization experiment. Both methods possess crystallization dynamics favorable for maximizing crystal size and we used them to facilitate the growth of large crystals, validating these approaches for membrane protein crystallization for NMX.

Original languageEnglish
Title of host publicationNeutron Crystallography in Structural Biology
EditorsPeter C.E. Moody
Number of pages22
Publication date2020
Publication statusPublished - 2020
SeriesMethods in Enzymology


  • Crystallization techniques
  • Membrane protein structure
  • MX
  • Neutron diffraction
  • NMX
  • Protein crystallography
  • Structural biology


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