Author Correction: NS2 induces an influenza A RNA polymerase hexamer and acts as a transcription to replication switch.

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Cryo-EM structure of DNA polymerase of African swine fever virus.

African swine fever virus (ASFV) is one of the most important causative agents of animal diseases and can cause highly fatal diseases in swine. ASFV DNA polymerase (DNAPol) is responsible for genome replication and highly conserved in all viral genotypes showing an ideal target for drug development. Here, we systematically determined the structures of ASFV DNAPol in apo, replicating and editing states.

NS2 induces an influenza A RNA polymerase hexamer and acts as a transcription to replication switch.

Genome transcription and replication of influenza A virus (FluA), catalyzed by viral RNA polymerase (FluAPol), are delicately controlled across the virus life cycle. A switch from transcription to replication occurring at later stage of an infection is critical for progeny virion production and viral non-structural protein NS2 has been implicated in regulating the switch. However, the underlying regulatory mechanisms and the structure of NS2 remained elusive for years.

Advances in Fatigue Performance of Metal Materials with Additive Manufacturing Based on Crystal Plasticity: A Comprehensive Review.

Using metal additive manufacturing processes can make up for traditional forging technologies when forming complex-shaped parts. At the same time, metal additive manufacturing has a fast forming speed and excellent manufacturing flexibility, so it is widely used in the aerospace industry and other fields. The fatigue strength of metal additive manufacturing is related to the microstructure of the epitaxially grown columnar grains and crystallographic texture.

Structure of monkeypox virus DNA polymerase holoenzyme.

The World Health Organization declared mpox (or monkeypox) a public health emergency of international concern in July 2022, and prophylactic and therapeutic measures are in urgent need. The monkeypox virus (MPXV) has its own DNA polymerase F8, together with the processive cofactors A22 and E4, constituting the polymerase holoenzyme for genome replication. Here, we determined the holoenzyme structure in complex with DNA using cryo-electron microscopy at the global resolution of ~2.