Premium
Membrane‐protein crystals for neutron diffraction
Author(s) -
Sørensen Thomas Lykke-Møller,
Hjorth-Jensen Samuel John,
Oksanen Esko,
Andersen Jacob Lauwring,
Olesen Claus,
Møller Jesper Vuust,
Nissen Poul
Publication year - 2018
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798318012561
Subject(s) - neutron diffraction , nucleation , crystal (programming language) , protein crystallization , crystallography , membrane , neutron , chemistry , materials science , crystal structure , physics , computer science , crystallization , nuclear physics , biochemistry , organic chemistry , programming language
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.