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ABSTRACT AST3-2 is the second of the three Antarctic Survey Telescopes, aimed at wide-field time-domain optical astronomy. It is located at Dome A, Antarctica, which is by many measures the best optical astronomy site on the Earth’s surface. Here we present the data from the AST3-2 automatic survey in 2016 and the photometry results. The median 5σ limiting magnitude in i-band is 17.8 mag and the light-curve precision is 4 mmag for bright stars. The data release includes photometry for over 7 million stars, from which over 3500 variable stars were detected, with 70 of them newly discovered. We classify these new variables into different types by combining their light-curve features with stellar properties from surveys such as StarHorse. 

The microstructure of FeCuB ribbons (∼20 μm thick) was modified to fabricate α′′-Fe 16 N 2 at a temperature as low as 160 °C. The ribbon samples were heat treated first at a temperature reaching 930 °C and then quenched down to room temperature. During the heat treatment, ribbon samples were oxidized, and hydrogen reduction was then conducted to remove the oxygen from the ribbon samples. The reduced ribbon samples had a porous structure, which improved the nitrogen diffusion efficiency and decreased the fabrication temperature of α′′-Fe 16 N 2 down to 160 °C. It was demonstrated that the techniques for microstructure control in this method including oxidation and reduction helped obtain the α′′-Fe 16 N 2 phase with high coercivity, thus manifesting this could be a promising technique for low-temperature nitridation on ribbons in general. 

Abstract Protein tyrosineO-sulfation (PTS) plays a crucial role in extracellular biomolecular interactions that dictate various cellular processes. It also involves in the development of many human diseases. Regardless of recent progress, our current understanding of PTS is still in its infancy. To promote and facilitate relevant studies, a generally applicable method is needed to enable efficient expression of sulfoproteins with defined sulfation sites in live mammalian cells. Here we report the engineering, in vitro biochemical characterization, structural study, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding of sulfotyrosine in mammalian cells. We further apply this chemical biology tool to cell-based studies on the role of a sulfation site in the activation of chemokine receptor CXCR4 by its ligand. Our work will not only facilitate cellular studies of PTS, but also paves the way for economical production of sulfated proteins as therapeutic agents in mammalian systems.