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The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 Å. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10° rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain...
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