ABSTRACT
Crystal and solution structures of fourteen ribosomal proteins from thermophilic bacteria have been determined during the last decade. This paper reviews structural studies of ribosomal proteins from Thermus thermophilus carried out at the Institute of Protein Research (Pushchino, Russia) in collaboration with the University of Lund (Lund, Sweden) and the Center of Structural Biochemistry (Karolinska Institute, Huddinge, Sweden). New experimental data on the crystal structure of the ribosomal protein L30 from T. thermophilus are also included.
Subject(s)
Bacterial Proteins/chemistry , Ribosomal Proteins/chemistry , Thermus thermophilus/chemistry , Bacterial Proteins/metabolism , Binding Sites , RNA/metabolism , Ribosomal Proteins/metabolismABSTRACT
Ribosomal protein L30 from Thermus thermophilus was overexpressed in E. coli cells. The recombinant protein was isolated and crystallized. The crystals belong to the spatial group P3(1) 12, and their crystallographic parameters are not different from those of crystals obtained earlier from the ribosomal protein isolated from T. thermophilus.
