Overexpression, purification and crystallization of tyrosyl-tRNA synthetase from the hyperthermophilic archaeon Aeropyrum pernix K1

被引：4

作者：

Iwaki, J

Suzuki, R

Fujimoto, Z ^{[1
]}

Momma, M

Kuno, A

Hasegawa, T

机构：

[1] Natl Inst Agrobiol Sci, Dept Biochem, Tsukuba, Ibaraki 3058602, Japan

[2] Yamagata Univ, Fac Sci, Dept Mat & Biol Chem, Yamagata 9908560, Japan

[3] Natl Inst Adv Ind Sci & Technol, Res Ctr Glycosci, Tsukuba, Ibaraki 3058566, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷

关键词：

D O I：

10.1107/S1744309105033245

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Hyperthermophilic archaeal tyrosyl-tRNA synthetase from Aeropyrum pernix K1 was cloned and overexpressed in Escherichia coli. The expressed protein was purified by Cibacron Blue affinity chromatography following heat treatment at 363 K. Crystals suitable for X-ray diffraction studies were obtained under optimized crystallization conditions in the presence of 1.5 M ammonium sulfate using the hanging-drop vapour-diffusion method. The crystals belonged to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 66.1, c = 196.2 angstrom, and diffracted to beyond 2.15 angstrom resolution at 100 K.

引用

页码：1003 / 1005

页数：3

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