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

Authors
Zhu, JP Chen, BZ Gong, WB Liang, YH Wang, HC Xu, Q Chen, ZL Lu, GY
Citation
Jp. Zhu et al., Crystallization and preliminary crystallographic studies of antibacterial polypeptide LCl expressed in Escherichia coli, ACT CRYST D, 57, 2001, pp. 1931-1932
Citations number
10
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
12
Pages
1931 - 1932
Database
ISI
SICI code
0907-4449(200112)57:<1931:CAPCSO>2.0.ZU;2-F
Abstract
LCI is a type of novel antibacterial polypeptide secreted by a Bacillus sub tilis strain. It consists of 47 residues with a molecular weight of 5468 Da . Using bioengineering, LCI was expressed in Escherichia coli DH5 alpha wit h recombinant plasmid pBVAB16. It was crystallized using PEG 4000 as a prec ipitant. The crystal belongs to space group P6(2)22 or P6(4)22, with unit-c ell parameters a=b=29.30, c=187.09 Angstrom, and diffracts to 2.44 Angstrom . A set of diffraction data to 2.8 Angstrom was collected.