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

TY - JOUR

T1 - Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli

AU - Bøgestrand, S

AU - Wiborg, O

AU - Thirup, S

AU - Nyborg, J

PY - 1995

Y1 - 1995

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Amino Acids

KW - Base Sequence

KW - Cloning, Molecular

KW - Crystallography, X-Ray

KW - DNA Primers

KW - Escherichia coli

KW - Mass Spectrometry

KW - Molecular Sequence Data

KW - Peptide Elongation Factors

KW - Protein Conformation

KW - Recombinant Proteins

KW - Trypsin

M3 - Journal article

C2 - 7615087

SN - 0014-5793

VL - 368

SP - 49

EP - 54

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -