Abstract
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 P21 symmetry that diffracted to 2.5 Å resolution which are suitable for high- resolution X-ray crystallographic analysis.
| Original language | English |
|---|---|
| Pages (from-to) | 112-114 |
| Number of pages | 3 |
| Journal | Journal of structural biology |
| Volume | 120 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 1 1997 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
Cite this
Crystallization and preliminary X-ray crystallographic study of the ribosomal protein S7 from Bacillus stearothermophilus. / Harada, Nao; Sano, Kazunari; Kimura, Makoto; Hosaka, Harumi; Nakagawa, Atushi; Tanaka, Isao.
In: Journal of structural biology, Vol. 120, No. 1, 01.01.1997, p. 112-114.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic study of the ribosomal protein S7 from Bacillus stearothermophilus
AU - Harada, Nao
AU - Sano, Kazunari
AU - Kimura, Makoto
AU - Hosaka, Harumi
AU - Nakagawa, Atushi
AU - Tanaka, Isao
PY - 1997/1/1
Y1 - 1997/1/1
N2 - 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 P21 symmetry that diffracted to 2.5 Å resolution which are suitable for high- resolution X-ray crystallographic analysis.
AB - 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 P21 symmetry that diffracted to 2.5 Å resolution which are suitable for high- resolution X-ray crystallographic analysis.
UR - http://www.scopus.com/inward/record.url?scp=0031257472&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031257472&partnerID=8YFLogxK
U2 - 10.1006/jsbi.1997.3907
DO - 10.1006/jsbi.1997.3907
M3 - Article
VL - 120
SP - 112
EP - 114
JO - Journal of Structural Biology
JF - Journal of Structural Biology
SN - 1047-8477
IS - 1
ER -