A new crystal form of the complex between seryl‐tRNA synthetase and tRNASer from Thermus thermophilus that diffracts to 2.8 Å resolution

FEBS Letters

Biou, V.¹  Tukalo, M.A.²  Berthet-Colominas, C.¹  Yaremchuk, A.D.²  Krikliviy, I.²  Cusack, S.¹  Malchenko, N.² 

[1] European Molecular Biology Laboratory, Grenoble Outstation, c/o ILL, 156X, 38042 Grenoble, France;Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukraine, 252627 Kiev, Ukraine

关键词: Aminoacyl-tRNA synthetase;    tRNA;    Protein-RNA complex;    Crystallization;    Thermus thermophilus;   

DOI  :  10.1016/0014-5793(92)81319-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two distinct complexes between seryl-tRNA synthetase and tRNA ^Ser from Thermus themophilus have been crystallized using ammonium sulphate as a precipitant. Form III crystals grow from solutions containing a 1:2.5 stoichiometry of synthetase dimer to tRNA. They are of monoclinic space group C2 with unit cell dimensions a = 211.6 Å, b = 126.8 Å, c = 197.1 Å, β = 132.4° and diffract to about 3.5 Å. Preliminary crystallographic results show that the crystallographic asymmetric unit contains two synthetase dimers. Form IV crystals grow from solutions containing a 1:1.5 stoichiometry of synthetase dimer to tRNA. They are of orthorhombic space group P2₁2₁2₁ with unit cell dimensions a = 124.5 Å, b = 128.9 Å, c = 121.2 Å and diffract to 2.8 Å resolution. Preliminary crystallographic results show that these crystals contain only one tRNA molecule bound to a synthetase dimer.

【 授权许可】

Unknown