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Membrane-protein crystals for neutron diffraction

Sørensen, Thomas Lykke Møller; Hjorth-Jensen, Samuel John LU ; Oksanen, Esko LU ; Andersen, Jacob Lauwring; Olesen, Claus; Møller, Jesper Vuust and Nissen, Poul (2018) In Acta Crystallographica Section D: Structural Biology2016-01-01+01:00 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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Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
membrane-protein crystallization, neutron macromolecular crystallography, SERCA1, structural biology
in
Acta Crystallographica Section D: Structural Biology2016-01-01+01:00
volume
74
issue
12
pages
11 pages
publisher
John Wiley and Sons Inc.
external identifiers
  • scopus:85059497526
ISSN
0907-4449
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
2019-02-20 11:44:14
@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         = {0907-4449},
  keyword      = {membrane-protein crystallization,neutron macromolecular crystallography,SERCA1,structural biology},
  language     = {eng},
  number       = {12},
  pages        = {1208--1218},
  publisher    = {John Wiley and Sons Inc.},
  series       = {Acta Crystallographica Section D: Structural Biology2016-01-01+01:00},
  title        = {Membrane-protein crystals for neutron diffraction},
  url          = {http://dx.doi.org/10.1107/S2059798318012561},
  volume       = {74},
  year         = {2018},
}