Crystallization and preliminary X-ray crystallographic study of the ribosomal protein S7 from Bacillus stearothermophilus.
Overproduction and crystallization of Bacillus stearothermophilus ribosomal 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 protein BstS7 was expressed in the cytoplasmic fraction of the E. coli cells and purified to homogeneity. This recombinant BstS7 was used to produce crystals with P2(1) symmetry that diffracted to 2.5 A resolution which are suitable for high-resolution X-ray crystallographic analysis.
Harada
N
N
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Sano
K
K
Kimura
M
M
Hosaka
H
H
Nakagawa
A
A
Tanaka
I
I
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D001411:Geobacillus stearothermophilus; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000302:isolation & purification
D011994:Recombinant Proteins; D012269:Ribosomal Proteins; C037442:ribosomal protein S7