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Preparation, crystallization and preliminary X-ray analysis of protein YtlP from Bacillus subtilis

Publiceringsår: 2006
Språk: Engelska
Sidor: 967-969
Publikation/Tidskrift/Serie: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00
Volym: 62
Nummer: 10
Dokumenttyp: Artikel i tidskrift
Förlag: Wiley-Blackwell


Bacillus subtilis YtlP is a protein that is predicted to belong to the bacterial and archael 2'-5' RNA-ligase family. It contains 183 residues and two copies of the HXTX sequence motif conserved among proteins belonging to this family. In order to determine the structure of YtlP and to compare it with the paralogue YjcG and identified 2'-5' RNA ligases, the gene ytlP was amplified from B. subtilis genomic DNA and cloned into expression vector pET-21a. The soluble protein was produced in Escherichia coli, purified to homogeneity and crystals suitable for X-ray analysis were obtained. The crystal diffracted to 2.0 angstrom and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.16, b = 48.54, c = 105.75 angstrom.


  • Microbiology
  • Biochemistry and Molecular Biology
  • 2′-5′ RNA-ligase family


  • ISSN: 2053-230X

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