Crystallization and preliminary X-ray analysis of the archaeosine tRNA-guanine transglycosylase from Pyrococcus horikoshii

被引：5

作者：

Ishitani, R

Nureki, O

Kijimoto, T

Watanabe, M

Kondo, H

Nameki, N

Okada, N

Nishimura, S

Yokoyama, S ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Tokyo, Japan

[2] SPring 8, RIKEN, Harima Inst, Mikazuki, Japan

[3] RIKEN, Genom Sci Ctr, Wako, Saitama, Japan

[4] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Biol Sci, Tokyo, Japan

[5] Merck, Banyu Tsukuba Res Inst, Tsukuba, Ibaraki, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444901011994

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The archaeosine tRNA-guanine transglycosylase from the hyperthermophilic archaeon Pyrococcus horikoshii was crystallized and preliminary X-ray characterization was performed. Single crystals were grown by the hanging-drop vapour-diffusion method, using sodium/potassium phosphate and sodium acetate as precipitants. The space group is P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 99.28 (14), c = 363.74 (56) Angstrom. The cryocooled crystals diffracted X-rays beyond 2.2 Angstrom resolution using synchrotron radiation from station BL44XU at SPring-8 (Harima). Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the MAD phasing method.

引用

页码：1659 / 1662

页数：4

共 34 条

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