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

Journal Article · Sun Oct 01 04:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S174430910603199X· OSTI ID:22356377

Liu, Cong; Li, Dan ^[1]; Hederstedt, Lars ^[2]; Li, Lanfen; Liang, Yu-He; Su, Xiao-Dong ^[1]

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1. National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871 (China)
2. Department of Cell and Organism Biology, Microbiology, Lund University, Lund SE-22362 (Sweden)

The crystallization and preliminary X-ray crystallographic analysis of protein YtlP from B. subtilis is reported. 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 Å and belonged to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 34.16, b = 48.54, c = 105.75 Å.

• OSTI ID: 22356377
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 10 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

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