TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic study of a 23S rRNA binding domain of the ribosomal protein L2 from Bacillus stearothermophilus
AU - Nakashima, Takashi
AU - Kimura, Makoto
AU - Nakagawa, Atsushi
AU - Tanaka, Isao
N1 - Funding Information:
We thank Professor N. Sakabe, Dr. N. Watanabe, Dr. M. Suzuki, and Dr. N. Igarashi of the Photon Factory for their kind help in data collection. We also thank Mr. H. Sugimoto, Miss M. Tanigu-chi, and Miss H. Hosaka of Hokkaido University for their kind help in data collection and processing. The Kyushu group thanks Professor N. Yamasaki (Kyushu University) for his encourage- ment and interest in the research. This work was supported in part by a grant-in-aid from the Ministry of Education, Science and Culture of Japan. A.N. and I.T. are members of the TARA project of the University of Tsukuba, Japan.
PY - 1998/12
Y1 - 1998/12
N2 - Ribosomal protein L2 from Bacillus stearothermophilus, a single polypeptide chain with 275 amino acid residues, is a primary 23S rRNA- binding protein in the large ribosomal subunit. Crystals of a 23S rRNA binding domain (BstL2-RBD: positions 60201) of the ribosomal protein L2 from B. stearothermophilus overexpressed in Escherichia coli have been grown in 0.1 M MES (pH 6.5) containing 15% polyethylene glycol 20 000. The crystals diffract to 2.3-Å resolution on a synchrotron X-ray source. The crystal belongs to the space group P1 and the unit cell axes are a = 28.05, b = 36.20, c = 69.74 Å α = 99.58°, β = 95.86°, and γ = 102.62°. There are two molecules of the BstL2-RBD in the asymmetric unit.
AB - Ribosomal protein L2 from Bacillus stearothermophilus, a single polypeptide chain with 275 amino acid residues, is a primary 23S rRNA- binding protein in the large ribosomal subunit. Crystals of a 23S rRNA binding domain (BstL2-RBD: positions 60201) of the ribosomal protein L2 from B. stearothermophilus overexpressed in Escherichia coli have been grown in 0.1 M MES (pH 6.5) containing 15% polyethylene glycol 20 000. The crystals diffract to 2.3-Å resolution on a synchrotron X-ray source. The crystal belongs to the space group P1 and the unit cell axes are a = 28.05, b = 36.20, c = 69.74 Å α = 99.58°, β = 95.86°, and γ = 102.62°. There are two molecules of the BstL2-RBD in the asymmetric unit.
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U2 - 10.1006/jsbi.1998.4053
DO - 10.1006/jsbi.1998.4053
M3 - Article
C2 - 9931278
AN - SCOPUS:0032419766
SN - 1047-8477
VL - 124
SP - 99
EP - 101
JO - Journal of structural biology
JF - Journal of structural biology
IS - 1
ER -