Nanomole-scale protein solid-state NMR by breaking intrinsic 1H T1 boundaries

We present an approach that accelerates protein solid-state NMR 5-20-fold using paramagnetic doping to condense datacollection time (to similar to 0.2 s per scan), overcoming a long-standing limitation on slow recycling owing to intrinsic H-1 T-1 longitudinal spin relaxation. Using low-power schemes under magic-angle spinning at 40 kHz, we obtained two-dimensional C-13-C-13 and C-13-N-15 solid-state NMR spectra for several to tens of nanomoles of beta-amyloid fibrils and ubiquitin in 1-2 d.