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The present work illustrates that small-angle neutron scattering, deuteration and contrast variation, combined with in vitro particle reconstruction, constitutes a very efficient approach to determine subunit architectures in large, symmetric protein complexes. In the case of the 468 kDa heterododecameric TET peptidase machine, it was demonstrated that the assembly of the 12 subunits is a highly controlled process and represents a way to optimize the catalytic efficiency of the enzyme.

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Specifically deuterated phospholipid bilayer nanodiscs have been developed which give a minimal contribution to neutron scattering data when used in 100% D2O. These provide an optimal platform for low-resolution structural determination of membrane proteins and their complexes in solution.
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