Crystallization and preliminary X-ray crystallographic study of a 23S rRNA binding domain of the ribosomal protein L2 from Bacillus stearothermophilus

Takashi Nakashima, Makoto Kimura, Atsushi Nakagawa, Isao Tanaka

研究成果: ジャーナルへの寄稿学術誌査読

5 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)99-101
ページ数3
ジャーナルJournal of structural biology
124
1
DOI
出版ステータス出版済み - 12月 1998

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学

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