Membrane-protein crystals for neutron diffraction
(2018) In Acta Crystallographica Section D: Structural Biology 74(12). p.1208-1218- 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... (More)
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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- author
- Sørensen, Thomas Lykke Møller ; Hjorth-Jensen, Samuel John LU ; Oksanen, Esko LU ; Andersen, Jacob Lauwring ; Olesen, Claus ; Møller, Jesper Vuust and Nissen, Poul
- organization
- publishing date
- 2018-12
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- membrane-protein crystallization, neutron macromolecular crystallography, SERCA1, structural biology
- in
- Acta Crystallographica Section D: Structural Biology
- volume
- 74
- issue
- 12
- pages
- 11 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:30605135
- scopus:85059497526
- ISSN
- 2059-7983
- DOI
- 10.1107/S2059798318012561
- language
- English
- LU publication?
- yes
- id
- eeb2adb5-f242-4047-a33a-31417a37fa1b
- date added to LUP
- 2019-01-23 13:06:47
- date last changed
- 2024-03-18 23:36:29
@article{eeb2adb5-f242-4047-a33a-31417a37fa1b,
abstract = {{<p>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.</p>}},
author = {{Sørensen, Thomas Lykke Møller and Hjorth-Jensen, Samuel John and Oksanen, Esko and Andersen, Jacob Lauwring and Olesen, Claus and Møller, Jesper Vuust and Nissen, Poul}},
issn = {{2059-7983}},
keywords = {{membrane-protein crystallization; neutron macromolecular crystallography; SERCA1; structural biology}},
language = {{eng}},
number = {{12}},
pages = {{1208--1218}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Acta Crystallographica Section D: Structural Biology}},
title = {{Membrane-protein crystals for neutron diffraction}},
url = {{http://dx.doi.org/10.1107/S2059798318012561}},
doi = {{10.1107/S2059798318012561}},
volume = {{74}},
year = {{2018}},
}