Crystals of Thermus thermophilus tRNA Asp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%.: Comparison with other aminoacylation systems

被引：4

作者：

Briand, C ^{[1
]}

Poterszman, A ^{[1
]}

Mitschler, A ^{[1
]}

Yusupov, M ^{[1
]}

Thierry, JC ^{[1
]}

Moras, D ^{[1
]}

机构：

[1] ULP, INSERM, CNRS, IGBMC,Lab Biol Struct,UPR 9004, F-67404 Illkirch Graffenstaden, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1998年 / 54卷

关键词：

D O I：

10.1107/S0907444998005800

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Thermus thermophilus tRNA(Asp), purified from a nonrecombinant source, has been crystallized ina-complex with its cognate dimeric (alpha 2) aspartyl-tRNA synthetase. Crystals diffract to 2.9 Angstrom resolution and belong to space group P6(3) with cell parameters a = b = 258, c = 90.9 Angstrom. The crystals contain one aspartyl-tRNA synthetase dimer and two tRNA molecules in the asymmetric unit, corresponding to a V-m of 4.85 Angstrom Da(-1) and 75% solvent content, When compared with those obtained for globular proteins these values are high, but fall within the range observed for other aminoacyl-tRNA Synthetases, either free or complexed with their tRNAs. A comparative survey is presented here.

引用

页码：1382 / 1386

页数：5

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