Crystallization and preliminary X-ray analysis of cecropin B from Bombyx mori

被引:2
作者
Liu, Zhongyuan [2 ,3 ]
Zhou, Qiangjun [4 ]
Mao, Xinfang [3 ]
Zheng, Xiangdong [2 ]
Guo, Jiubiao [2 ]
Zhang, Fuchun [3 ]
Wen, Tingyi [1 ]
Pang, Hai [2 ]
机构
[1] Chinese Acad Sci, Inst Microbiol, Dept Ind Microbiol & Biotechnol, Beijing 100101, Peoples R China
[2] Tsinghua Univ, Sch Med, Beijing 100084, Peoples R China
[3] Xinjiang Univ, Xinjiang Key Lab Biol Resources & Genet Engn, Urumqi 830046, Peoples R China
[4] Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2010年 / 66卷
基金
中国国家自然科学基金;
关键词
HELICAL ANTIMICROBIAL PEPTIDES; ORIENTED LIPID-BILAYERS; PORE-FORMING PEPTIDE; SOLID-STATE NMR; INSECT IMMUNITY; INNATE IMMUNITY; CONFORMATION; SPECTROSCOPY; ORIENTATION; MECHANISM;
D O I
10.1107/S1744309110020130
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Cecropin B is a 37-residue cationic antimicrobial peptide derived from the haemolymph of Bombyx mori. The precise mechanism by which cecropins exert their antimicrobial and cytolytic activities is not well understood. Crystals of cecropin B were obtained by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant at 289 K. The crystal diffracted to 1.43 angstrom resolution using X-ray radiation and belonged to the orthorhombic space group P1, with unit-cell parameters a = 15.08, b = 22.75, c = 30.20 angstrom, alpha = 96.9, beta = 103.1, gamma = 96.5 degrees. The asymmetric unit contained only one molecule of cecropin B, with a calculated Matthews coefficient of 2.48 angstrom(3) Da(-1) and a solvent content of 50.4%.
引用
收藏
页码:851 / 853
页数:3
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