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

Liu, Cong; Li, Dan; Hederstedt, Lars LU ; Li, Lanfen; Liang, Yu-He and Su, Xiao-Dong (2006) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications 62(10). p.967-969
Abstract
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.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
2′-5′ RNA-ligase family
in
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
volume
62
issue
10
pages
967 - 969
publisher
Wiley-Blackwell
external identifiers
  • pmid:17012785
  • wos:000240912700006
  • scopus:33749526126
ISSN
2053-230X
DOI
10.1107/S174430910603199X
language
English
LU publication?
yes
id
b522f603-7fe9-4ff1-80ab-037dbb4142ad (old id 389880)
date added to LUP
2007-10-09 08:10:02
date last changed
2019-02-20 07:24:47
@article{b522f603-7fe9-4ff1-80ab-037dbb4142ad,
  abstract     = {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.},
  author       = {Liu, Cong and Li, Dan and Hederstedt, Lars and Li, Lanfen and Liang, Yu-He and Su, Xiao-Dong},
  issn         = {2053-230X},
  keyword      = {2′-5′ RNA-ligase family},
  language     = {eng},
  number       = {10},
  pages        = {967--969},
  publisher    = {Wiley-Blackwell},
  series       = {Acta Crystallographica. Section F: Structural Biology and Crystallization Communications},
  title        = {Preparation, crystallization and preliminary X-ray analysis of protein YtlP from <em>Bacillus subtilis</em>},
  url          = {http://dx.doi.org/10.1107/S174430910603199X},
  volume       = {62},
  year         = {2006},
}