The spliceosome is a macromolecular machine that carries out the excision o
f introns from eukaryotic pre-mRNAs and splicing together of exons. Four la
rge RNA-protein complexes, called the U1, U2, U4/U6 and U5 small nuclear ri
bonucleoprotein particles (snRNPs), and some non-snRNf proteins assemble ar
ound three short conserved sequences within the intron in an ordered manner
to form the active spliceosome. We aim to provide insight into the molecul
ar details of the mechanism of pre-mRNA splicing through crystallographic s
tudies of the snRNPs. We have solved the X-ray crystal structure of some sn
RNP proteins as part of either protein-protein complexes or RNA-protein com
plexes. These structures have provided an important insight into the overal
l architecture of the U1 and U2 snRNPs and the mechanisms of RNA-protein an
d protein-protein recognition.