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Incorporating mesopores into ZSM-5 zeolite to form a hierarchical structure has been regarded as an important approach to enhance the diffusivity and catalyst lifetime for light alkane aromatization. Herein, hierarchical ZSM-5 nano-aggregated microspheres were simply and directly synthesized and characterized using TPAOH as a single template without any mesoporous templates or zeolite seeds. The size of the ZSM-5 microspheres and the distribution of mesopores could be regulated by controlling the alkalinity of the synthesis gel. A possible self-assembly mechanism was proposed based on tracing the formation process of ZSM-5 microspheres with crystallization time. The ZSM-5 microspheres modified with Zn were applied in n-hexane aromatization and exhibited better catalytic stability than conventional mono-dispensed microporous ZSM-5 due to the existence of accessible mesopores. [ABSTRACT FROM AUTHOR]

Feline infectious peritonitis virus (FIPV) causes a lethal systemic granulomatous disease in wild and domestic cats around the world. Currently, no effective vaccines or drugs have been developed against it. As a member of the genus Alphacoronavirus, FIPV encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of FIPV in complex with a Michael acceptor-type inhibitor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space group I422, with unit-cell parameters a = 112.3, b = 112.3, c = 102.1 Å. There is one molecule per asymmetric unit. [ABSTRACT FROM AUTHOR]

Porcine epidemic diarrhea virus (PEDV) mainly infects neonatal pigs, resulting in significant morbidity and mortality. Owing to problems such as long periods of virus shedding, existing vaccines cannot provide complete protection from PEDV infection. The PEDV genome encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of Porcine epidemic diarrhea virus in complex with a Michael acceptor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space group R3, with unit-cell parameters a = 175.3, b = 175.3, c = 58.7 Å. Two molecules were identified per asymmetric unit. [ABSTRACT FROM AUTHOR]

Human coronavirus NL63 mainly infects younger children and causes cough, fever, rhinorrhoea, bronchiolitis and croup. It encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome-encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of human coronavirus NL63 was crystallized in complex with a Michael acceptor. The complex crystals diffracted to 2.85 Å resolution and belonged to space group P41212, with unit-cell parameters a = b = 87.2, c = 212.1 Å. Two molecules were identified per asymmetric unit. [ABSTRACT FROM AUTHOR]