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Crystallization and preliminary diffraction studies of the structural domain E of Thermus flavus 5S rRNA.
Nolte, A; Klussman, S; Lorenz, S; Bald, R; Betzel, C; Dauter, Z; Wilson, K; Fürste, J P; Erdmann, V A.
Affiliation
  • Nolte A; Institut für Biochemie, Freie Universität Berlin, Germany.
FEBS Lett ; 374(2): 292-4, 1995 Oct 30.
Article in En | MEDLINE | ID: mdl-7589556
ABSTRACT
The ribosomal 5S RNA is an essential constituent of the large ribosomal subunit. To overcome the difficulties of crystallizing large RNA molecules such as 5S rRNAs, we decided to divide the 5S rRNA in five domains A through E to determine their structure. Recently we determined the crystal structural of the helical domain A. Here we report the crystallization of the chemically synthesized domain E of the Thermus flavus 5S rRNA. The crystal form is trigonal with unit cell dimensions a = b = 42.80 A and c = 162.20 A. Diffraction-data to 2.8 A have been recorded and the structure solution is currently underway by means of MIR and MAD techniques.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Thermus / RNA, Ribosomal, 5S / Nucleic Acid Conformation Language: En Journal: FEBS Lett Year: 1995 Document type: Article Affiliation country: Germany
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Collection: 01-internacional Database: MEDLINE Main subject: Thermus / RNA, Ribosomal, 5S / Nucleic Acid Conformation Language: En Journal: FEBS Lett Year: 1995 Document type: Article Affiliation country: Germany