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 DH5alpha with recombinant plasmid pBVAB16. It was crystallized using PEG 4000 as a precipitant. The crystal belongs to space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 29.30, c = 187.09 A, and diffracts to 2.44 A. A set of diffraction data to 2.8 A was collected.
Zhu
J P
JP
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Chen
B Z
BZ
Gong
W B
WB
Liang
Y H
YH
Wang
H C
HC
Xu
Q
Q
Chen
Z L
ZL
Lu
G Y
GY
D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D001412:Bacillus subtilis / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D010455:Peptides; D011487:Protein Conformation
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C444362:antibacterial polypeptide LCI