Crystallization and preliminary crystallographic studies of antibacterial polypeptide LCI expressed inEscherichia coli
| Autor: | Bingzhang Chen, Guang-Ying Lu, Weibin Gong, Huan-Chen Wang, Yu-He Liang, Qing Xu, Zhang-Liang Chen, Jia-Peng Zhu |
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| Rok vydání: | 2001 |
| Předmět: |
Protein Conformation
Bacillus subtilis Biology Crystallography X-Ray medicine.disease_cause law.invention QH301 Structural Biology law PEG ratio Escherichia coli medicine Crystallization QA Antibacterial polypeptide LCI Strain (chemistry) General Medicine biology.organism_classification Anti-Bacterial Agents Crystallography Biochemistry Recombinant DNA bacteria Peptides Antimicrobial Cationic Peptides |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 57:1931-1932 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444901017280 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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