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

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)99-101
Number of pages3
JournalJournal of structural biology
Volume124
Issue number1
DOIs
Publication statusPublished - Dec 1 1998

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Geobacillus stearothermophilus
Crystallization
Large Ribosome Subunits
X-Rays
Synchrotrons
Carrier Proteins
Escherichia coli
Amino Acids
Peptides
ribosomal protein L2
IgA receptor

All Science Journal Classification (ASJC) codes

  • Structural Biology

Cite this

Crystallization and preliminary X-ray crystallographic study of a 23S rRNA binding domain of the ribosomal protein L2 from Bacillus stearothermophilus. / Nakashima, Takashi; Kimura, Makoto; Nakagawa, Atsushi; Tanaka, Isao.

In: Journal of structural biology, Vol. 124, No. 1, 01.12.1998, p. 99-101.

Research output: Contribution to journalArticle

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