Crystallization of mutant forms of the γ subunit of archaeal translation initiation factor 2

Archaeal translation initiation factor 2 (aIF2) is homologous to its eukaryotic counterpart (eIF2). It is a heterotrimeric protein consisting of α, β, and γ subunits. The protein e/aIF2 forms a ternary complex with guanosine 5′-triphosphate and the initiator methionyl-tRNA (Met-tRNA_i) and delivers the latter to the ribosome. In archaea, translation initiation factor 2 has an additional function. The γ subunit of aIF2 binds mRNAs with a triphosphate at the 5′-end and prevents 5′-to-3′ directional mRNA decay. To determine the mRNA-binding site on the surface of aIF2γ, mutations were introduced into the protein sequence at sites of possible interactions with mRNA. The crystals of the mutant forms of aIF2γ were obtained, and X-ray diffraction data sets suitable for structure determination at atomic resolution were collected.     

Structural Investigations of RNA–Protein Complexes in Post-Ribosomal Era

Crystallography Reports - Structural studies of RNA–protein complexes are important for understanding many molecular mechanisms occurring in cells (e.g., regulation of protein synthesis and...     

Erratum to:Structural Investigations of RNA–Protein Complexes in Post-Ribosomal Era

Crystallography Reports - An Erratum to this paper has been published: https://doi.org/10.1134/S1063774521340095     

Role of the electric potential in the creep acceleration and formation of Al fracture surface

Aluminum creep acceleration at applying an electric potential to ±1 V has been established experimentally. The fracture surface and side surface microrelief near the fracture surface were investigated by scanning electron microscopy. It is shown that application of ±1 V potential leads to decrease in the fracture toughness. Possible reasons for this phenomenon are considered.     

Effect of the Ile222Thr Missense Mutation in SsoIF2γ on the Affinity of γ and β Subunits of aIF2

Crystallography Reports - Translation initiation factors 2 from eukaryotes (eIF2) and archaea (аIF2) mediate the delivery of charged initiator tRNA (Met-tRNAiMet) to the small ribosomal...