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Removal of nanometer-sized contaminant particles (CPs) from substrates is essential in successful fabrication of nanoscale devices. The particle beam technique that uses nanometer-sized bullet particles (BPs) moving at supersonic velocity was improved by operating it at room temperature to achieve higher velocity and size uniformity of BPs and was successfully used to remove CPs as small as 10 nm. CO2 BPs were generated by gas-phase nucleation and growth in a supersonic nozzle; appropriate size and velocity of the BPs were obtained by optimizing the nozzle contours and CO2/He mixture fraction. Cleaning efficiency greater than 95% was attained. BP velocity was the most important parameter affecting removal of CPs in the 10-nm size range. Compared to cryogenic Ar or N2 particles, CO2 BPs were more uniform in size and had higher velocity and, therefore, cleaned CPs more effectively.

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A structural protein of SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2), nucleocapsid (N) protein is phosphorylated by glycogen synthase kinase (GSK)-3 on the serine/arginine (SR) rich motif located in disordered regions. Although phosphorylation by GSK-3β constitutes a critical event for viral replication, the molecular mechanism underlying N phosphorylation is not well understood. In this study, we found the putative alpha-helix L/FxxxL/AxxRL motif known as the GSK-3 interacting domain (GID), found in many endogenous GSK-3β binding proteins, such as Axins, FRATs, WWOX, and GSKIP. Indeed, N interacts with GSK-3β similarly to Axin, and Leu to Glu substitution of the GID abolished the interaction, with loss of N phosphorylation. The N phosphorylation is also required for its structural loading in a virus-like particle (VLP). Compared to other coronaviruses, N of Sarbecovirus lineage including bat RaTG13 harbors a CDK1primed phosphorylation site and Gly-rich linker for enhanced phosphorylation by GSK-3β. Furthermore, we found that the S202R mutant found in Delta and R203K/G204R mutant found in the Omicron variant allow increased abundance and hyper-phosphorylation of N. Our observations suggest that GID and mutations for increased phosphorylation in N may have contributed to the evolution of variants.

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