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• W1995610568 abstract "Peptidyl-tRNA is produced from the ribosome as a result of aborted translation. Peptidyl-tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl-tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2-methyl-2,4-pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67 Å, and diffracted X-rays to atomic resolution (beyond 1.0 Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (VM = 1.69 Å3 Da−1). The structure is being solved by molecular replacement." @default.
• W1995610568 created "2016-06-24" @default.
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• W1995610568 date "2013-02-27" @default.
• W1995610568 modified "2023-09-30" @default.
• W1995610568 title "Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from<i>Thermus thermophilus</i>HB8" @default.
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• W1995610568 doi "https://doi.org/10.1107/s1744309113003424" @default.
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