M. Garber et al., CRYSTALLIZATION AND STRUCTURAL STUDIES OF COMPONENTS OF THE PROTEIN-SYNTHESIZING SYSTEM FROM THERMUS-THERMOPHILUS, Journal of crystal growth, 168(1-4), 1996, pp. 301-307
A long-term program on crystallization and structural studies of the p
rotein synthesis machinery components from an extreme thermophile Ther
mus thermophilus was set up at the Institute of Protein Research (Russ
ia) about 15 years ago. These studies have recently revealed the struc
tures of elongation factor G, aspartyl-tRNA synthetase and ribosomal p
roteins S6 and L1. Different components of the protein synthesis machi
nery from T. thermophilus are also being investigated in other groups
and many important results have been obtained recently. Here we descri
be only some special problems on crystal handling and non-isomorphism
that have been overcome during structural studies of EF-G and ribosoma
l proteins in our group. This paper presents also new data on the crys
tallization of ribosomal proteins S7, S8, S15, L22 and leucyl-tRNA syn
thetase from T. thermophilus.