Purification, crystallization and preliminary crystallographic analysis of the Hermes transposase

Zhanita N. Perez, Primrose Musingarimi, Nancy L. Craig, Fred Dyda, Alison Burgess Hickman

Research output: Contribution to journalArticlepeer-review

Abstract

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 Å resolution have been obtained at 277 K by the hanging-drop method.

Original languageEnglish (US)
Pages (from-to)587-590
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number6
DOIs
StatePublished - 2005

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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