Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-TΨC domain of tRNA.
[No authors listed]
摘要
Peptidyl-tRNA hydrolase (Pth) cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are the product of aborted translation. In the present work, Pth from Escherichia coli was crystallized with the acceptor-TΨC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space group P6(1), with unit-cell parameters a = b = 55.1, c = 413.1 à , and diffracted X-rays beyond 2.4 à resolution. The asymmetric unit is expected to contain two complexes of Pth and the acceptor-TΨC domain of tRNA (V(M) = 2.8 à (3) Da(-1)), with a solvent content of 60.8%. The structure is being solved by molecular replacement.
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基因功能
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原始数据
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文献解读
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