Reinforcement learning in cold atom experiments.

Cold atom traps are at the heart of many quantum applications in science and technology. The preparation and control of atomic clouds involves complex optimization processes, that could be supported and accelerated by machine learning. In this work, we introduce reinforcement learning to cold atom experiments and demonstrate a flexible and adaptive approach to control a magneto-optical trap.

Multiplane Diffractive Acoustic Networks.

Acoustic holograms are able to control pressure fields with high spatial resolution, enabling complex fields to be projected with minimal hardware. This capability has made holograms attractive tools for applications, including manipulation, fabrication, cellular assembly, and ultrasound therapy. However, the performance benefits of acoustic holograms have traditionally come at the cost of temporal control.

C Proteins Have a Common Origin and a Common Structural Organization.

The protein C is a small viral protein encoded in an overlapping frame of the P gene in the subfamily Orthoparamyxovirinae. This protein, expressed by alternative translation initiation, is a virulence factor that regulates viral transcription, replication, and production of defective interfering RNA, interferes with the host-cell innate immunity systems and supports the assembly of viral particles and budding. We expressed and purified full-length and an N-terminally truncated C protein from Tupaia paramyxovirus (TupV) C protein (genus Narmovirus).

Bichromatic state-dependent disordered potential for Anderson localization of ultracold atoms.

Abstract: The ability to load ultracold atoms at a well-defined energy in a disordered potential is a crucial tool to study quantum transport, and in particular Anderson localization. In this paper, we present a new method for achieving that goal by rf transfer of atoms in an atomic Bose-Einstein condensate from a disorder-insensitive state to a disorder-sensitive state. It is based on a bichromatic laser speckle pattern, produced by two lasers whose frequencies are chosen so that their light-shifts cancel each other in the first state and add up in the second state.

Structural Dynamics of the C-terminal X Domain of Nipah and Hendra Viruses Controls the Attachment to the C-terminal Tail of the Nucleocapsid Protein.

To understand the dynamic interactions between the phosphoprotein (P) and the nucleoprotein (N) within the transcription/replication complex of the Paramyxoviridae and to decipher their roles in regulating viral multiplication, we characterized the structural properties of the C-terminal X domain (P) of Nipah (NiV) and Hendra virus (HeV) P protein. In crystals, isolated NiV P adopted a two-helix dimeric conformation, which was incompetent for binding its partners, but in complex with the C-terminal intrinsically disordered tail of the N protein (N), it folded into a canonical 3H bundle conformation. In solution, SEC-MALLS, SAXS and NMR spectroscopy experiments indicated that both NiV and HeV P were larger in size than expected for compact proteins of the same molecular mass and were in conformational exchange between a compact three-helix (3H) bundle and partially unfolded conformations, where helix α is detached from the other two.