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

Författare

Summary, in English

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.

Publiceringsår

2006

Språk

Engelska

Sidor

967-969

Publikation/Tidskrift/Serie

Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

Volym

62

Issue

10

Dokumenttyp

Artikel i tidskrift

Förlag

Wiley-Blackwell

Ämne

  • Microbiology
  • Biochemistry and Molecular Biology

Nyckelord

  • 2′-5′ RNA-ligase family

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 2053-230X