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

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

Acta crystallographica. Section F, Structural biology and crystallization communications (2010-07-08)
Zhongyuan Liu, Qiangjun Zhou, Xinfang Mao, Xiangdong Zheng, Jiubiao Guo, Fuchun Zhang, Tingyi Wen, Hai Pang
ABSTRACT

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 A 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 A, 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 A(3) Da(-1) and a solvent content of 50.4%.

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Sigma-Aldrich
Cecropin B, ≥97% (HPLC), powder