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

Cong Liu; Dan Li; Lars Hederstedt; Lanfen Li; Yu-He Liang; Xiao-Dong Su

doi:10.1107/S174430910603199X

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

Cong Liu, Dan Li, Lars Hederstedt, Lanfen Li, Yu-He Liang, Xiao-Dong Su

Peking University

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	967-969
Journal	Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	10
DOIs	https://doi.org/10.1107/S174430910603199X
Publication status	Published - 2006

Subject classification (UKÄ)

Microbiology
Biological Sciences

Free keywords

2′-5′ RNA-ligase family

Access to Document

10.1107/S174430910603199X

Cite this

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

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.",

keywords = "2′-5′ RNA-ligase family",

author = "Cong Liu and Dan Li and Lars Hederstedt and Lanfen Li and Yu-He Liang and Xiao-Dong Su",

year = "2006",

doi = "10.1107/S174430910603199X",

language = "English",

volume = "62",

pages = "967--969",

journal = "Acta Crystallographica. Section F: Structural Biology and Crystallization Communications",

issn = "2053-230X",

publisher = "John Wiley & Sons Inc.",

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TY - JOUR

T1 - Preparation, crystallization and preliminary X-ray analysis of protein YtlP from Bacillus subtilis

AU - Liu, Cong

AU - Li, Dan

AU - Hederstedt, Lars

AU - Li, Lanfen

AU - Liang, Yu-He

AU - Su, Xiao-Dong

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - 2′-5′ RNA-ligase family

U2 - 10.1107/S174430910603199X

DO - 10.1107/S174430910603199X

M3 - Article

SN - 2053-230X

VL - 62

SP - 967

EP - 969

JO - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

IS - 10

ER -

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

Abstract

Subject classification (UKÄ)

Free keywords

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