Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli.
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.
Bøgestrand
S
S
Department of Chemistry, Aarhus University, Denmark.
Wiborg
O
O
Thirup
S
S
Nyborg
J
J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001483:Base Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D017931:DNA Primers; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D014357:Trypsin
D000596:Amino Acids; D017931:DNA Primers; D010445:Peptide Elongation Factors; D011994:Recombinant Proteins; C023512:elongation factor Ts; D014357:Trypsin