Crystallization and preliminary X-ray analysis of cecropin B from Bombyx mori
AUTHORS
Liu
ZZhongyuan ,
Zhou
QQiangjun ,
Mao
XXinfang ,
Zheng
XXiangdong ,
Guo
JJiubiao ,
Zhang
FFuchun ,
Wen
TTingyi ,
Pang
HHai .
Acta crystallographica. Section F, Structural biology and crystallization communications. 2010 7 1; 66(Pt 7).
851-3
- PMID: 20606290[PubMed].
- PMCID: PMC2898478.
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%.
Tags: 2010