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Article Dans Une Revue Acta Crystallograph Sect F Struct Biol Cryst Commun Année : 2007

Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase.

Résumé

Human mitochondrial tyrosyl-tRNA synthetase and a truncated version with its C-terminal S4-like domain deleted were purified and crystallized. Only the truncated version, which is active in tyrosine activation and Escherichia coli tRNA(Tyr) charging, yielded crystals suitable for structure determination. These tetragonal crystals, belonging to space group P4(3)2(1)2, were obtained in the presence of PEG 4000 as a crystallizing agent and diffracted X-rays to 2.7 A resolution. Complete data sets could be collected and led to structure solution by molecular replacement.

Dates et versions

hal-00167519 , version 1 (21-08-2007)

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Citer

Luc Bonnefond, Magali Frugier, Elodie Touzé, Bernard Lorber, Catherine Florentz, et al.. Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase.. Acta Crystallograph Sect F Struct Biol Cryst Commun, 2007, 63 (Pt 4), pp.338-41. ⟨10.1107/S1744309107012481⟩. ⟨hal-00167519⟩

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