Status of UCN Source at WWR-M Reactor

The WWR-M reactor at PNPI is going to be equipped with an ultacold neutron source of high density. Method of UCN production is based on their accumulation in the super fluid helium due to particular qualities of that quantum liquid. The possibility of maintaining the temperature T = 1.371K with a thermal load of P = 60W was shown experimentally, while the theoretical load is expected to be P=30W. The project envisages the installation on UCN beams the experimental setups of various research projects such as searching for the nEDM, measure the neutron lifetime, and the observation of neutron to antineutron oscillation. In addition to UCN beams, three beams of cold and verycold neutrons are planned. Six experimental setups will be installed on these beams. At present, a vacuum container of the UCN source has been manufactured and the manufacture of low-temperature deuterium and helium parts of the source has been started

Structural basis for GPCR-independent activation of heterotrimeric Gi proteins.

Heterotrimeric G proteins are key molecular switches that control cell behavior. The canonical activation of G proteins by agonist-occupied G protein-coupled receptors (GPCRs) has recently been elucidated from the structural perspective. In contrast, the structural basis for GPCR-independent G protein activation by a novel family of guanine-nucleotide exchange modulators (GEMs) remains unknown. Here, we present a 2.0-Å crystal structure of Gαi in complex with the GEM motif of GIV/Girdin. Nucleotide exchange assays, molecular dynamics simulations, and hydrogen-deuterium exchange experiments demonstrate that GEM binding to the conformational switch II causes structural changes that allosterically propagate to the hydrophobic core of the Gαi GTPase domain. Rearrangement of the hydrophobic core appears to be a common mechanism by which GPCRs and GEMs activate G proteins, although with different efficiency. Atomic-level insights presented here will aid structure-based efforts to selectively target the noncanonical G protein activation