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

FEBS Letters

Bøgestrand, Søren¹  Nyborg, Jens¹  Wiborg, Ove¹  Thirup, Søren¹ 

[1] Division of Biostructural Chemistry, Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark

关键词: Protein biosynthesis;    Nucleotide exchange factor;    Elongation factor Ts;    Trypsin fragments;    Crystallization;    Pseudo symmetry;    Escherichia coli;   

DOI  :  10.1016/0014-5793(95)00597-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 P2₁. 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.

【 授权许可】

Unknown