Crystallization and preliminary X-ray diffraction studies of intact EF-Tu from Thermus aquaticus YT-1.
نویسندگان
چکیده
Many attempts have been made to elucidate the three-dimensional structure from elongation factor Tu, but so far the only crystals suitable for X-ray crystallography contained a partially degraded protein. Here, we report the crystallization of a fully active, intact EF-Tu from thermus aquaticus. The crystals belong to hexagonal space group P6(3)(22) and diffract up to 2.6 A. The cell dimensions are a = b = 178 A, c = 238 A and 6 molecules are contained per asymmetric unit.
منابع مشابه
The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
BACKGROUND Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS The crystal structure of EF-Tu from Thermus aquaticus, complexe...
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ورودعنوان ژورنال:
- FEBS letters
دوره 240 1-2 شماره
صفحات -
تاریخ انتشار 1988