Suppression of electron spin decoherence of the diamond NV center by a transverse magnetic field

We demonstrate that the spin decoherence of nitrogen vacancy (NV) centers in diamond can be suppressed by a transverse magnetic field if the electron spin bath is the primary decoherence source. The NV spin coherence, created in "a decoherence-free subspace" is protected by the transverse component of the zero-field splitting, increasing the spin-coherence time about twofold. The decoherence due to the electron spin bath is also suppressed at magnetic fields stronger than ~25 gauss when applied parallel to the NV symmetry axis. Our method can be used to extend the spin-coherence time of similar spin systems for applications in quantum computing, field sensing, and other metrologies.Comment: 20 pages, 4 figure

Measurement of Untruncated Nuclear Spin Interactions via Zero- to Ultra-Low-Field Nuclear Magnetic Resonance

Zero- to ultra-low-field nuclear magnetic resonance (ZULF NMR) provides a new regime for the measurement of nuclear spin-spin interactions free from effects of large magnetic fields, such as truncation of terms that do not commute with the Zeeman Hamiltonian. One such interaction, the magnetic dipole-dipole coupling, is a valuable source of spatial information in NMR, though many terms are unobservable in high-field NMR, and the coupling averages to zero under isotropic molecular tumbling. Under partial alignment, this information is retained in the form of so-called residual dipolar couplings. We report zero- to ultra-low-field NMR measurements of residual dipolar couplings in acetonitrile-2-$^{13}$C aligned in stretched polyvinyl acetate gels. This represents the first investigation of dipolar couplings as a perturbation on the indirect spin-spin $J$-coupling in the absence of an applied magnetic field. As a consequence of working at zero magnetic field, we observe terms of the dipole-dipole coupling Hamiltonian that are invisible in conventional high-field NMR. This technique expands the capabilities of zero- to ultra-low-field NMR and has potential applications in precision measurement of subtle physical interactions, chemical analysis, and characterization of local mesoscale structure in materials.Comment: 6 pages, 3 figure

Genetically encoded reporters for hyperpolarized xenon magnetic resonance imaging

Magnetic resonance imaging (MRI) enables high-resolution non-invasive observation of the anatomy and function of intact organisms. However, previous MRI reporters of key biological processes tied to gene expression have been limited by the inherently low molecular sensitivity of conventional ^1H MRI. This limitation could be overcome through the use of hyperpolarized nuclei, such as in the noble gas xenon, but previous reporters acting on such nuclei have been synthetic. Here, we introduce the first genetically encoded reporters for hyperpolarized ^(129)Xe MRI. These expressible reporters are based on gas vesicles (GVs), gas-binding protein nanostructures expressed by certain buoyant microorganisms. We show that GVs are capable of chemical exchange saturation transfer interactions with xenon, which enables chemically amplified GV detection at picomolar concentrations (a 100- to 10,000-fold improvement over comparable constructs for ^1H MRI). We demonstrate the use of GVs as heterologously expressed indicators of gene expression and chemically targeted exogenous labels in MRI experiments performed on living cells

Dynamic nuclear polarization at 9 T using a novel 250 GHz gyrotron microwave source

In this communication, we report enhancements of nuclear spin polarization by dynamic nuclear polarization (DNP) in static and spinning solids at a magnetic field strength of 9 T (250 GHz for g = 2 electrons, 380 MHz for [superscript 1]H). In these experiments, [superscript 1]H enhancements of up to 170 ± 50 have been observed in 1-[superscript 13]C-glycine dispersed in a 60:40 glycerol/water matrix at temperatures of 20 K; in addition, we have observed significant enhancements in [superscript 15]N spectra of unoriented pf1-bacteriophage. Finally, enhancements of ~17 have been obtained in two-dimensional [superscript 13]C–[superscript 13]C chemical shift correlation spectra of the amino acid U–[superscript 13]C, [superscript 15]N-proline during magic angle spinning (MAS), demonstrating the stability of the DNP experiment for sustained acquisition and for quantitative experiments incorporating dipolar recoupling. In all cases, we have exploited the thermal mixing DNP mechanism with the nitroxide radical 4-amino-TEMPO as the paramagnetic dopant. These are the highest frequency DNP experiments performed to date and indicate that significant signal enhancements can be realized using the thermal mixing mechanism even at elevated magnetic fields. In large measure, this is due to the high microwave power output of the 250 GHz gyrotron oscillator used in these experiments.Natural Sciences and Engineering Research Council of Canada (Postgraduate Scholarship Fellowship)National Institutes of Health (U.S.) (Grant GM-35382)National Institutes of Health (U.S.) (Grant GM-55327)National Institutes of Health (U.S.) (Grant RR-00995

DNP Enhanced Frequency-Selective TEDOR Experiments in Bacteriorhodopsin

We describe a new approach to multiple [superscript 13]C–[superscript 15]N distance measurements in uniformly labeled solids, frequency-selective (FS) TEDOR. The method shares features with FS-REDOR and ZF- and BASE-TEDOR, which also provide quantitative [superscript 15]N–[superscript 13]C spectral assignments and distance measurements in U-[[superscript 13]C,[superscript 15]N] samples. To demonstrate the validity of the FS-TEDOR sequence, we measured distances in [U-[superscript 13]C,15N]-asparagine which are in good agreement with other methods. In addition, we integrate high frequency dynamic nuclear polarization (DNP) into the experimental protocol and use FS-TEDOR to record a resolved correlation spectrum of the Arg-[superscript 13]Cγ–[superscript 15]Nε region in [U-[superscript 13]C,15N]-bacteriorhodopsin. We resolve six of the seven cross-peaks expected based on the primary sequence of this membrane protein.National Institute of Biomedical Imaging and Bioengineering (U.S.) (Grant Number EB-001960)National Institute of Biomedical Imaging and Bioengineering (U.S.) (Grant Number EB-002804)National Institute of Biomedical Imaging and Bioengineering (U.S.) (Grant Number EB-001035)National Institute of Biomedical Imaging and Bioengineering (U.S.) (Grant Number EB-002026

Room Temperature Operation of a Radiofrequency Diamond Magnetometer near the Shot Noise Limit

We operate a nitrogen vacancy (NV-) diamond magnetometer at ambient temperatures and study the dependence of its bandwidth on experimental parameters including optical and microwave excitation powers. We introduce an analytical theory that yields an explicit formula for the response of an ensemble of NV- spins to an oscillating magnetic field, such as in NMR applications. We measure a detection bandwidth of 1.6 MHz and a sensitivity of 4.6 nT/Hz^(1/2), unprecedented in a detector with this active volume and close to the photon shot noise limit of our experiment.Comment: 4 pages; 4 figures; supporting informatio

Resolution and Polarization Distribution in Cryogenic DNP/MAS Experiments

This contribution addresses four potential misconceptions associated with high-resolution dynamic nuclear polarization/magic angle spinning (DNP/MAS) experiments. First, spectral resolution is not generally compromised at the cryogenic temperatures at which DNP experiments are performed. As we demonstrate at a modest field of 9 T (380 MHz [superscript 1]H), 1 ppm linewidths are observed in DNP/MAS spectra of a membrane protein in its native lipid bilayer, and <0.4 ppm linewidths are reported in a crystalline peptide at 85 K. Second, we address the concerns about paramagnetic broadening in DNP/MAS spectra of proteins by demonstrating that the exogenous radical polarizing agents utilized for DNP are distributed in the sample in such a manner as to avoid paramagnetic broadening and thus maintain full spectral resolution. Third, the enhanced polarization is not localized around the polarizing agent, but rather is effectively and uniformly dispersed throughout the sample, even in the case of membrane proteins. Fourth, the distribution of polarization from the electron spins mediated via spin diffusion between [superscript 1]H–[superscript 1]H strongly dipolar coupled spins is so rapid that shorter magnetization recovery periods between signal averaging transients can be utilized in DNP/MAS experiments than in typical experiments performed at ambient temperature.National Institutes of Health (U.S.) (Grant EB002804)National Institutes of Health (U.S.) (Grant EB003151)National Institutes of Health (U.S.) (Grant EB002026)National Institutes of Health (U.S.) (Grant EB001965)National Institutes of Health (U.S.) (Grant EB004866)National Science Foundation (U.S.). Graduate Research Fellowship Progra