PMID:7615087

Citation	Bøgestrand, S, Wiborg, O, Thirup, S and Nyborg, J (1995) Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli. FEBS Lett. 368:49-54
Abstract	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.
Links	PubMed
Keywords	Amino Acid Sequence; Amino Acids/analysis; Base Sequence; Cloning, Molecular; Crystallography, X-Ray; DNA Primers; Escherichia coli/chemistry; Escherichia coli/genetics; Mass Spectrometry; Molecular Sequence Data; Peptide Elongation Factors/chemistry; Peptide Elongation Factors/genetics; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Trypsin
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