Purification, crystallization and preliminary crystallographic analysis of the Hermes transposase

被引:6
作者
Perez, ZN
Musingarimi, P
Craig, NL
Dyda, F
Burgess, A
Hickman, AB [1 ]
机构
[1] NIDDK, Mol Biol Lab, Bethesda, MD 20892 USA
[2] Johns Hopkins Univ, Sch Med, Howard Hughes Med Inst, Dept Mol Biol & Genet, Baltimore, MD 21205 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷
关键词
D O I
10.1107/S1744309105015721
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
DNA transposition is the movement of a defined segment of DNA from one location to another. Although the enzymes that catalyze transposition in bacterial systems have been well characterized, much less is known about the families of transposase enzymes that function in higher organisms. Active transposons have been identified in many insect species, providing tools for gene identification and offering the possibility of altering the genotypes of natural insect populations. One of these active transposons is Hermes, a 2749-base-pair element from Musca domestica that encodes its own transposase. An N-terminally deleted version of the Hermes transposase (residues 79-612) has been overexpressed and purified, and crystals that diffract to 2.1 angstrom resolution have been obtained at 277 K by the hanging-drop method.
引用
收藏
页码:587 / 590
页数:4
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