Preparation, crystallization and preliminary X-ray analysis of protein YtlP fromBacillus subtilis
| Autor: | Xiao-Dong Su, Cong Liu, Lan-Fen Li, Dan Li, Yu-He Liang, Lars Hederstedt |
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| Rok vydání: | 2006 |
| Předmět: |
Molecular Sequence Data
Biophysics Bacillus subtilis Biology Crystallography X-Ray medicine.disease_cause Biochemistry chemistry.chemical_compound Bacterial Proteins Structural Biology Genetics medicine Amino Acid Sequence Cloning Molecular Escherichia coli Gene Expression vector RNA Condensed Matter Physics biology.organism_classification Polynucleotide Ligases genomic DNA chemistry Crystallization Communications Crystallization Sequence motif Sequence Alignment DNA |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:967-969 |
| ISSN: | 1744-3091 |
| Popis: | 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 A and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.16, b = 48.54, c = 105.75 A. |
| Databáze: | OpenAIRE |
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