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Crystallization and preliminary diffraction studies of the structural domain E of Thermus flavus 2S rRNA
Author(s) -
Nolte Alexis,
Kluβman Sven,
Lorenz Siegfried,
Bald Rolf,
Betzel Christian,
Dauter Zbigniev,
Wilson Keith,
Fürste Jens Peter,
Erdmann Volker A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01136-3
Subject(s) - thermus thermophilus , ribosomal rna , crystallization , crystallography , rna , crystal structure , 5s ribosomal rna , domain (mathematical analysis) , 50s , chemistry , biology , ribosome , biochemistry , 18s ribosomal rna , escherichia coli , gene , organic chemistry , mathematics , mathematical analysis
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: and . Diffraction‐data to 2.8 Å have been recorded and the structure solution is currently underway by means of MIR and MAD techniques.