Engineering Crystal Packing in RNA-Protein Complexes II: A Historical Perspective from the Structural Studies of the Spliceosome

Abstract

Cryo-electron microscopy has greatly advanced our understanding of how the spliceosome cycles through different conformational states to conduct the chemical reactions that remove introns from pre-mRNA transcripts. The Cryo-EM structures were built upon decades of crystallographic studies of various spliceosomal RNA-protein complexes. In this review we give an overview of the crystal structures solved in the Nagai group, utilizing many of the strategies to design crystal packing as described in the accompanying paper.

Structural studies of the spliceosome: Bridging the gaps

“…The dynamics and complexity of the splicing machinery posed a great challenge for structural studies, in particular by X-ray crystallography, which required extensive engineering of RNAs, proteins and crystal contacts [ 2 ]. Developments in electron cryo-microscopy (cryo-EM) have overcome these limitations and paved the way towards the first high-resolution structures of fully assembled spliceosomes [ 3 , 4 , 5 , 6 ].…”