Crystallization of actophorin, an actin filament-severing protein from Acanthamoeba.
نویسندگان
چکیده
Actophorin is an actin monomer-binding and actin filament-severing protein from Acanthamoeba castellanii. It crystallizes out of polyethylene glycol in a form suitable for high resolution x-ray analysis. The crystals are orthorhombic and have the symmetry of the space group P2(1)2(1)2(1) with lattice constants a = 39.8 +/- 0.5, b = 47.3 +/- 0.6, and c = 69.9 +/- 1.6 A. They diffract to a resolution of at least 2.8 A, and the asymmetric unit contains one actophorin monomer of Mr 15,000.
منابع مشابه
Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
Actophorin is an abundant 15-kD actinbinding protein from Acanthamoeba that is thought to form a nonpolymerizable complex with actin monomers and also to reduce the viscosity of polymerized actin by severing filaments (Cooper et al., 1986. J. Biol. Chem. 261:477-485). Homologous proteins have been identified in sea urchin, chicken, and mammalian tissues. Chemical crosslinking produces a 1:1 cov...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 263 34 شماره
صفحات -
تاریخ انتشار 1988