No abstract

We have investigated the influence of impurities on the possible supersolid transition by systematically enriching isotopically-pure 4 He (< 1 ppb of 3 He) with 3 He. The onset of nonclassical rotational inertia is broadened and shifts monotonically to higher temperature with increasing 3 He concentration, suggesting that the phenomenon is correlated to the condensation of 3 He atoms onto the dislocation network in solid 4 He.

Liquid 4He enters the superfluid state and flows without friction below 2.176 K. Thin liquid films adsorbed on solid substrates undergo the same transformation, although at a lower temperature. When the substrate is subjected to oscillatory motion a portion of the film, known as the superfluid fraction, decouples from the oscillation. A similar phenomenon has been observed in solid 4He, in which a fraction of the solid seems to decouple from the motion of the surrounding lattice. Although this observation has been replicated in various laboratories, no thermodynamic signature of the possible supersolid transition has been seen. Here we report the finding of a heat capacity peak that coincides with the onset of mass decoupling. This complementary experimental evidence supports the existence of a genuine transition between the normal solid and supersolid phases of 4He.

The emergence of SARS-CoV-2 infection has posed unprecedented threat to global public health. The virus-encoded non-structural protein 14 (nsp14) is a bi-functional enzyme consisting of an exoribonuclease (ExoN) domain and a methyltransferase (MTase) domain and plays a pivotal role in viral replication. Here, we report the structure of SARS-CoV-2 nsp14-ExoN domain bound to its co-factor nsp10 and show that, compared to the SARS-CoV nsp10/nsp14-full-length complex, SARS-CoV-2 nsp14-ExoN retains an integral exoribonuclease fold and preserves an active configuration in the catalytic center. Analysis of the nsp10/nsp14-ExoN interface reveals a footprint in nsp10 extensively overlapping with that observed in the nsp10/nsp16 structure. A marked difference in the co-factor when engaging nsp14 and nsp16 lies in helix-α1′, which is further experimentally ascertained to be involved in nsp14-binding but not in nsp16-engagement. Finally, we also show that nsp10/nsp14-ExoN is enzymatically active despite the absence of nsp14-MTase domain. These data demonstrate that SARS-CoV-2 nsp10/nsp14-ExoN functions as an exoribonuclease with both structural and functional integrity.

Highlights d RABV-G ecto-domain protein structure is revealed using a fusion-loop substitution strategy d Crystal structures of RABV-G at both basic and acidic pHs are solved d Structural comparison reveals basis of pH-dependent structural transitions in RABV-G d Complex structure shows 523-11 antibody binds a bipartite epitope for neutralization