✦ LIBER ✦

Solving the structure of Escherichia coli elongation factor Tu using a twinned data set

✍ Scribed by Heffron, Susan E. ;Moeller, Rhonda ;Jurnak, Frances

Book ID: 104478199
Publisher: International Union of Crystallography
Year: 2006
Tongue: English
Weight: 727 KB
Volume: 62
Category: Article
ISSN: 0907-4449
DOI: 10.1107/s0907444906004021

No coin nor oath required. For personal study only.

✦ Synopsis

Escherichia coli elongation factor Tu-GDP (EF-Tu-GDP) was crystallized in the presence of novel inhibitors. The only crystals which could be grown were epitaxially as well as merohedrally twinned, highly mosaic and diffracted to a resolution of 3.4 A ˚in space group P3 1 21, with unit-cell parameters a = b = 69.55, c = 169.44 A ˚, = = 90, = 120 . To determine whether an inhibitor was present in the crystal, a poor-quality X-ray diffraction data set had to be processed. The three-dimensional structure was ultimately solved and the original question answered. The results also reveal a new type of dimer packing for EF-Tu-GDP.

📜 SIMILAR VOLUMES

A secondary promoter for elongation fact

A secondary promoter for elongation factor Tu synthesis in the str ribosomal protein operon of Escherichia coli

✍ Zengel, Janice M. ;Lindahl, Lasse 📂 Article 📅 1982 🏛 Springer 🌐 English ⚖ 646 KB

The str operon of Escherichia coli contains genes for ribosomal proteins S12 and S7 and for elongation factors EF-G and EF-Tu (Jaskunas et al. 1975). We have subcloned various segments of DNA from this operon onto multicopy plasmids. We found that cells carrying a recombinant plasmid which lacks the