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

doi:10.1107/S2059798318012561

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

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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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.

Original language	English
Journal	Acta crystallographica Section D: Structural biology
Volume	74
Issue	Pt 12
Pages (from-to)	1208-1218
Number of pages	11
ISSN	2059-7983
DOIs	https://doi.org/10.1107/S2059798318012561
Publication status	Published - 1 Dec 2018

Keywords

SERCA1
membrane-protein crystallization
neutron macromolecular crystallography
structural biology

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10.1107/S2059798318012561

membrane-protein_crystals_for_neutron_diffraction-op5obwe0hqdwcbqp0rw2ye5tcrbmxxaqOther version, 1.18 MBLicence: Other

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title = "Membrane-protein crystals for neutron diffraction",

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.",

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Membrane-protein crystals for neutron diffraction. / Sørensen, Thomas Lykke Møller; Hjorth-Jensen, Samuel John; Oksanen, Esko et al.
In: Acta crystallographica Section D: Structural biology , Vol. 74, No. Pt 12, 01.12.2018, p. 1208-1218.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Membrane-protein crystals for neutron diffraction

AU - Sørensen, Thomas Lykke Møller

AU - Hjorth-Jensen, Samuel John

AU - Oksanen, Esko

AU - Andersen, Jacob Lauwring

AU - Olesen, Claus

AU - Møller, Jesper Vuust

AU - Nissen, Poul

PY - 2018/12/1

Y1 - 2018/12/1

N2 - 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.

AB - 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.

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KW - membrane-protein crystallization

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DO - 10.1107/S2059798318012561

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SN - 2059-7983

VL - 74

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EP - 1218

JO - Acta crystallographica Section D: Structural biology

JF - Acta crystallographica Section D: Structural biology

IS - Pt 12

ER -

Membrane-protein crystals for neutron diffraction

Abstract

Keywords

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