Geometric quenching of orbital pair breaking in a single crystalline superconducting nanomesh network

In a superconductor Cooper pairs condense into a single state and in so doing support dissipation free charge flow and perfect diamagnetism. In a magnetic field the minimum kinetic energy of the Cooper pairs increases, producing an orbital pair breaking effect. We show that it is possible to significantly quench the orbital pair breaking effect for both parallel and perpendicular magnetic fields in a thin film superconductor with lateral nanostructure on a length scale smaller than the magnetic length. By growing an ultra-thin (2 nm thick) single crystalline Pb nanowire network, we establish nm scale lateral structure without introducing weak links. Our network suppresses orbital pair breaking for both perpendicular and in-plane fields with a negligible reduction in zero-field resistive critical temperatures. Our study opens a frontier in nanoscale superconductivity by providing a strategy for maintaining pairing in strong field environments in all directions with important technological implications

Design and performance of an ultrahigh vacuum spectroscopic-imaging scanning tunneling microscope with a hybrid vibration isolation system

A spectroscopic imaging-scanning tunneling microscope (SI-STM) allows the atomic scale visualization of surface electronic and magnetic structure of novel quantum materials with high energy resolution. To achieve the optimal performance, low vibration facility is required. Here, we describe the design and the performance of an ultrahigh vacuum STM system supported by a hybrid vibration isolation system that consists of a pneumatic passive and a piezoelectric active vibration isolation stages. The STM system is equipped with a 1K pot cryogenic insert and a 9 Tesla superconducting magnet, capable of continuous SI-STM measurements for 7 days. A field ion microscopy system is installed for in situ STM tip treatment. We present the detailed vibrational noise analysis of the hybrid vibration isolation system and demonstrate the performance of our STM system by taking high resolution spectroscopic maps and topographic images on several quantum materials. Our results establish a new strategy to achieve an effective vibration isolation system for high-resolution STM and other scanning probe microscopy to investigate the nanoscale quantum phenomena

Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins

The RecA family of proteins mediates homologous recombination, an evolutionarily conserved pathway that maintains genomic stability by protecting against DNA double strand breaks. RecA proteins are thought to facilitate DNA strand exchange reactions as closed-rings or as right-handed helical filaments. Here, we report the crystal structure of a left-handed Sulfolobus solfataricus RadA helical filament. Each protomer in this left-handed filament is linked to its neighbour via interactions of a β-strand polymerization motif with the neighbouring ATPase domain. Immediately following the polymerization motif, we identified an evolutionarily conserved hinge region (a subunit rotation motif) in which a 360° clockwise axial rotation accompanies stepwise structural transitions from a closed ring to the AMP–PNP right-handed filament, then to an overwound right-handed filament and finally to the left-handed filament. Additional structural and functional analyses of wild-type and mutant proteins confirmed that the subunit rotation motif is crucial for enzymatic functions of RecA family proteins. These observations support the hypothesis that RecA family protein filaments may function as rotary motors

Three New Structures of Left-Handed RadA Helical Filaments: Structural Flexibility of N-Terminal Domain Is Critical for Recombinase Activity

RecA family proteins, including bacterial RecA, archaeal RadA, and eukaryotic Dmc1 and Rad51, mediate homologous recombination, a reaction essential for maintaining genome integrity. In the presence of ATP, these proteins bind a single-strand DNA to form a right-handed nucleoprotein filament, which catalyzes pairing and strand exchange with a homologous double-stranded DNA (dsDNA), by as-yet unknown mechanisms. We recently reported a structure of RadA left-handed helical filament, and here present three new structures of RadA left-handed helical filaments. Comparative structural analysis between different RadA/Rad51 helical filaments reveals that the N-terminal domain (NTD) of RadA/Rad51, implicated in dsDNA binding, is highly flexible. We identify a hinge region between NTD and polymerization motif as responsible for rigid body movement of NTD. Mutant analysis further confirms that structural flexibility of NTD is essential for RadA's recombinase activity. These results support our previous hypothesis that ATP-dependent axial rotation of RadA nucleoprotein helical filament promotes homologous recombination