New Insights into Ribosome Structure and Function.

In the past 4 years, because of the advent of new cameras, many ribosome structures have been solved by cryoelectron microscopy (cryo-EM) at high, often near-atomic resolution, bringing new mechanistic insights into the processes of translation initiation, peptide elongation, termination, and recycling. Thus, cryo-EM has joined X-ray crystallography as a powerful technique in structural studies of translation. The significance of this new development is that structures of ribosomes in complex with their functional binding partners can now be determined to high resolution in multiple states as they perform their work.

Structure and assembly model for the Trypanosoma cruzi 60S ribosomal subunit.

Ribosomes of trypanosomatids, a family of protozoan parasites causing debilitating human diseases, possess multiply fragmented rRNAs that together are analogous to 28S rRNA, unusually large rRNA expansion segments, and r-protein variations compared with other eukaryotic ribosomes. To investigate the architecture of the trypanosomatid ribosomes, we determined the 2.5-Å structure of the Trypanosoma cruzi ribosome large subunit by single-particle cryo-EM.

Determination of the ribosome structure to a resolution of 2.5 Å by single-particle cryo-EM.

With the advance of new instruments and algorithms, and the accumulation of experience over decades, single-particle cryo-EM has become a pivotal part of structural biology. Recently, we determined the structure of a eukaryotic ribosome at 2.5 Å for the large subunit.

Coupled affinity and sizing chromatography: a novel in-process analytical tool to measure titer and trend Fc-protein aggregation.

The expanding use of monoclonal antibodies in the biopharmaceuticals industry has brought the need for new analytical tools. We have developed a coupled affinity and gel-filtration high-performance liquid chromatography method to simultaneously analyze titer and quality of monoclonal antibodies. Before this assay, available analytical methods for protein aggregation required highly purified proteins.