Crystallization and structural studies of components of the protein-synthesizing system from Thermus thermophilus

Abstract A long-term program on crystallization and structural studies of the protein synthesis machinery components from an extreme thermophile Thermus thermophilus was set up at the Institute of Protein Research (Russia) about 15 years ago. These studies have recently revealed the structures of elongation factor G, aspartyl-tRNA synthetase and ribosomal proteins S6 and L1. Different components of the protein synthesis machinery from T.thermophilus are also being investigated in other groups and many important results have been obtained recently. Here we describe only some special problems on crystal handling and non-isomorphism that have been overcome during structural studies of EF-G and ribosomal proteins in our group. This paper presents also new data on the crystallization of ribosomal proteins S7, S8, S15, L22 and leucyl-tRNA synthetase from T.thermophilus .