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

Zhu, Jia-Peng and Chen, Bing-Zhang and Gong, Wei-Bin and Liang, Yu-He and Wang, Huan-Chen and Xu, Qing and Chen, Zhang-Liang and Lu, Guang-Ying (2001) Crystallization and preliminary crystallographic studies of antibacterial polypeptide LCI expressed in Escherichia coli. Acta Crystallographica Section D: Biological Crystallography, D57 (12). pp. 1931-1932. ISSN 0907-4449 (https://doi.org/10.1107/S0907444901017280)

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Abstract

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.

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