Crystallization and preliminary crystallographic studies of antibacterial polypeptide LCI expressed in Escherichia coli

LCI is a type of novel antibacterial polypeptide secreted by a Bacillus subtilis strain. It consists of 47 residues with a molecular weight of 5468 Da. Using bioengineering, LCI was expressed in Escherichia coli DH5α with recombinant plasmid pBVAB16. It was crystallized using PEG 4000 as a precipita...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-12, Vol.57 (12), p.1931-1932
Hauptverfasser:	Zhu, Jia-Peng, Chen, Bing-Zhang, Gong, Wei-Bin, Liang, Yu-He, Wang, Huan-Chen, Xu, Qing, Chen, Zhang-Liang, Lu, Guang-Ying
Format:	Artikel
Sprache:	eng
Schlagworte:	Anti-Bacterial Agents - chemistry antibacterial polypeptides Bacillus subtilis - chemistry Crystallization Crystallography, X-Ray Escherichia coli - genetics Peptides Protein Conformation
Online-Zugang:	Volltext
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Beschreibung
Zusammenfassung:	LCI is a type of novel antibacterial polypeptide secreted by a Bacillus subtilis strain. It consists of 47 residues with a molecular weight of 5468 Da. Using bioengineering, LCI was expressed in Escherichia coli DH5α with recombinant plasmid pBVAB16. It was crystallized using PEG 4000 as a precipitant. The crystal belongs to space group P6222 or P6422, with unit‐cell parameters a = b = 29.30, c = 187.09 Å, and diffracts to 2.44 Å. A set of diffraction data to 2.8 Å was collected.
ISSN:	1399-0047 0907-4449 1399-0047
DOI:	10.1107/S0907444901017280