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Preparation of a crystallizable mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.
- Source :
-
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2002 Oct; Vol. 58 (Pt 10 Pt 2), pp. 1871-3. Date of Electronic Publication: 2002 Sep 28. - Publication Year :
- 2002
-
Abstract
- SelB is a bacterial elongation factor required for the decoding of a UGA stop codon together with a specific mRNA hairpin to selenocysteine. In attempts to crystallize Moorella thermoacetica SelB, a proteolysis process occurred and crystals of a proteolytic fragment were observed. The crystals, which appeared after a year, contained a C-terminal 30 kDa fragment containing the mRNA-binding domain. This fragment was reproduced through recloning. Crystals diffracting to 2.7 A were obtained.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins genetics
Bacterial Proteins isolation & purification
Base Sequence
Binding Sites
Cloning, Molecular
Crystallography, X-Ray
DNA Primers
Nucleic Acid Conformation
Peptide Elongation Factors genetics
Peptide Elongation Factors isolation & purification
Peptide Fragments chemistry
Peptide Fragments isolation & purification
RNA, Messenger chemistry
RNA, Messenger genetics
Recombinant Proteins chemistry
Recombinant Proteins isolation & purification
Bacteria chemistry
Bacterial Proteins chemistry
Peptide Elongation Factors chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0907-4449
- Volume :
- 58
- Issue :
- Pt 10 Pt 2
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Publication Type :
- Academic Journal
- Accession number :
- 12351842
- Full Text :
- https://doi.org/10.1107/s090744490201380x