Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 70, Issue -, Pages 317-328Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1399004713027466
Keywords
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Funding
- European Spallation Source
- Danish Government
- Danish Research Council
- German Research Council [SFB 1052/B6]
- UK Engineering and Physical Sciences Research Council (EPSRC) [GR/R99393/01, EP/C015452/1]
- EU NMI3 programme under FP7
- EU CRISP programme [283745]
- EPSRC [EP/C015452/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [GR/R99393/01, EP/C015452/1] Funding Source: researchfish
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Structural studies of membrane proteins remain a great experimental challenge. Functional reconstitution into artificial nanoscale bilayer disc carriers that mimic the native bilayer environment allows the handling of membrane proteins in solution. This enables the use of small-angle scattering techniques for fast and reliable structural analysis. The difficulty with this approach is that the carrier discs contribute to the measured scattering intensity in a highly nontrivial fashion, making subsequent data analysis challenging. Here, an elegant solution to circumvent the intrinsic complexity brought about by the presence of the carrier disc is presented. In combination with small-angle neutron scattering (SANS) and the D,D2O/H2O-based solvent contrast-variation method, it is demonstrated that it is possible to prepare specifically deuterated carriers that become invisible to neutrons in 100% D2O at the length scales relevant to SANS. These 'stealth' carrier discs may be used as a general platform for low-resolution structural studies of membrane proteins using well established data-analysis tools originally developed for soluble proteins.
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