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Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli

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  • S Bøgestrand, Denmark
  • O Wiborg, Denmark
  • S Thirup
  • J Nyborg, Denmark
  • Centre for Psychiatric Research
  • Department of Molecular Biology
  • Department of Molecular Biology
A 25 kDa C-terminal tryptic fragment of elongation factor Ts has been purified to homogeneity. Experimental evidence suggests that the 25 kDa C-terminal and the 5.3 kDa N-terminal fragments are structurally independent domains. The N-terminal fragment is shown to be essential for the nucleotide exchange activity. Crystals of the C-terminal fragment belong to space group P2 or P2(1). The diffraction pattern shows a pronounced pseudo-C2 symmetry at low resolution. This pseudo symmetry increases when the crystals are irradiated with X-rays for a few hours.
Original languageEnglish
JournalF E B S Letters
Volume368
Issue1
Pages (from-to)49-54
Number of pages5
ISSN0014-5793
Publication statusPublished - 1995

    Research areas

  • Amino Acid Sequence, Amino Acids, Base Sequence, Cloning, Molecular, Crystallography, X-Ray, DNA Primers, Escherichia coli, Mass Spectrometry, Molecular Sequence Data, Peptide Elongation Factors, Protein Conformation, Recombinant Proteins, Trypsin

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