N. Harada et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC STUDY OF THE RIBOSOMAL-PROTEIN S7 FROM BACILLUS-STEAROTHERMOPHILUS, Journal of structural biology, 120(1), 1997, pp. 112-114
Overproduction and crystallization of Bacillus stearothermophilus ribo
somal protein S7 (BstS7), a primary 16S rRNA binding protein and also
a translational repressor protein, have been performed to analyze its
three-dimensional structure by X-ray crystallography. Ribosomal protei
n BstS7 was expressed in the cytoplasmic fraction of the E. coli cells
and purified to homogeneity. This recombinant BstS7 was used to produ
ce crystals with P2(1) symmetry that diffracted to 2.5 Angstrom resolu
tion which are suitable for high-resolution X-ray crystallographic ana
lysis. (C) 1997 Academic Press.