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 Angstrom were obtained.
Original language | English |
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Pages (from-to) | 1871-1873 |
Journal | Acta Crystallographica. Section D: Biological Crystallography |
Volume | 58 |
DOIs | |
Publication status | Published - 2002 |
Subject classification (UKÄ)
- Structural Biology