Precise characterization of Li-6 Feshbach resonances using trap-sideband-resolved RF spectroscopy of weakly bound molecules

We perform radio-frequency dissociation spectroscopy of weakly bound 6Li2 Feshbach molecules using low-density samples of about 30 molecules in an optical dipole trap. Combined with a high magnetic field stability, this allows us to resolve the discrete trap levels in the radio-frequency dissociation spectra. This novel technique allows the binding energy of Feshbach molecules to be determined with unprecedented precision. We use these measurements as an input for a fit to the 6Li scattering potential using coupled-channel calculations. From this new potential, we determine the pole positions of the broad 6Li Feshbach resonances with an accuracy better than 7×10-4 of the resonance widths. This eliminates the dominant uncertainty for current precision measurements of the equation of state of strongly interacting Fermi gases. As an important consequence, our results imply a corrected value for the Bertsch parameter ξ measured by Ku et al. [ Science 335 563 (2012)], which is ξ=0.370(5)(8)

Efimov physics from the functional renormalization group

Few-body physics related to the Efimov effect is discussed using the functional renormalization group method. After a short review of renormalization in its modern formulation we apply this formalism to the description of scattering and bound states in few-body systems of identical bosons and distinguishable fermions with two and three components. The Efimov effect leads to a limit cycle in the renormalization group flow. Recently measured three-body loss rates in an ultracold Fermi gas $^6$Li atoms are explained within this framework. We also discuss briefly the relation to the many-body physics of the BCS-BEC crossover for two-component fermions and the formation of a trion phase for the case of three species.Comment: 28 pages, 13 figures, invited contribution to a special issue of "Few-Body Systems" devoted to Efimov physics, published versio

Efimov Trimers near the Zero-crossing of a Feshbach Resonance

Near a Feshbach resonance, the two-body scattering length can assume any value. When it approaches zero, the next-order term given by the effective range is known to diverge. We consider the question of whether this divergence (and the vanishing of the scattering length) is accompanied by an anomalous solution of the three-boson Schr\"odinger equation similar to the one found at infinite scattering length by Efimov. Within a simple zero-range model, we find no such solutions, and conclude that higher-order terms do not support Efimov physics.Comment: 8 pages, no figures, final versio

Efimov physics beyond universality

We provide an exact solution of the Efimov spectrum in ultracold gases within the standard two-channel model for Feshbach resonances. It is shown that the finite range in the Feshbach coupling makes the introduction of an adjustable three-body parameter obsolete. The solution explains the empirical relation between the scattering length a_- where the first Efimov state appears at the atom threshold and the van der Waals length l_vdw for open channel dominated resonances. There is a continuous crossover to the closed channel dominated limit, where the scale in the energy level diagram as a function of the inverse scattering length 1/a is set by the intrinsic length r* associated with the Feshbach coupling. Our results provide a number of predictions for non-universal ratios between energies and scattering lengths that can be tested in future experiments.Comment: 6 pages, 4 figures; final versio

MTO1 mediates tissue-specificity of OXPHOS defects via tRNA modification and translation optimization, which can be bypassed by dietary intervention.

Mitochondrial diseases often exhibit tissue-specific pathologies, but this phenomenon is poorly understood. Here we present regulation of mitochondrial translation by the Mitochondrial Translation Optimization Factor 1, MTO1, as a novel player in this scenario. We demonstrate that MTO1 mediates tRNA modification and controls mitochondrial translation rate in a highly tissue specific manner associated with tissue-specific OXPHOS defects. Activation of mitochondrial proteases, aberrant translation products, as well as defects in OXPHOS complex assembly observed in MTO1 KO mice further imply that MTO1 impacts translation fidelity. In our mouse model, MTO1-related OXPHOS deficiency can be bypassed by feeding a ketogenic diet. This therapeutic intervention is independent of the MTO1-mediated tRNA modification and involves balancing of mitochondrial and cellular secondary stress responses. Our results thereby establish mammalian MTO1 as a novel factor in the tissue-specific regulation of OXPHOS and fine-tuning of mitochondrial translation accuracy