X-ray structures of eIF5B and the eIF5B-eIF1A complex: the conformational flexibility of eIF5B is restricted on the ribosome by interaction with eIF1A.

eIF5B and eIF1A are two translation-initiation factors that are universally conserved among all kingdoms. They show a unique interaction in eukaryotes which is important for ribosomal subunit joining. Here, the structures of two isolated forms of yeast eIF5B and of the eIF5B-eIF1A complex (eIF1A and eIF5B do not contain the respective N-terminal domains) are reported.

[Validation study on a multi-residue method for determination of pesticide residues in agricultural products by new automatic pretreatment equipment (FASRAC) and GC-MS/MS].

A validation study was performed on a multiresidue method for determination of pesticide residues in agricultural products according to the method validation guideline of the Ministry of Health, Labour and Welfare of Japan. FASRAC (Food Automatic Analytical Systems for Residual Agricultural Chemicals) automatically performs extraction of pesticide residues from agricultural products with acetonitrile, filtration, constant volume, mixing with the use of air, mixing acetonitrile with buffer solvent, separation, and dehydration with sodium sulfate. The extract was purified with a GC/NH2 column.

Crystallization and preliminary X-ray crystallographic analysis of eIF5BΔN and the eIF5BΔN-eIF1AΔN complex.

The binding between two universally conserved translation initiation factors, eIF5B and eIF1A, is important in the initiation step of eukaryotic protein synthesis on the ribosome. Through this interaction, eIF1A assists in recruiting eIF5B to the initiating 40S subunit; eIF5B then encourages the joining of the 60S subunit to form an initiating 80S ribosome. Here, the expression, purification, crystallization and preliminary X-ray analyses of eIF5BΔN and the eIF5BΔN-eIF1AΔN complex from Saccharomyces cerevisiae are reported.