Hennig M, Schlesier B, Pfeffer S, Höhne W E
Institute of Biochemistry, Humboldt University, Berlin, GDR.
J Mol Biol. 1990 Oct 5;215(3):339-40. doi: 10.1016/s0022-2836(05)80354-7.
A seed globulin from Vicia narbonensis L. has been crystallized by vapour diffusion induced pH-shift. Crystals are suitable for high-resolution X-ray structural analysis and diffract to better than 1.5 A. Narbonin crystallizes in the monoclinic space group P21 with alpha = 46.9 A, b = 75.5 A, c = 50.9 A, alpha = gamma = 90 degrees, beta = 120.5 degrees. The protein consists of one polypeptide chain that does not coincide with the subunits of legumin or vicilin after SDS/polyacrylamide gel electrophoresis and has a relative molecular mass of about 33,000.
通过蒸汽扩散诱导pH值变化,已使来自窄叶野豌豆的一种种子球蛋白结晶。晶体适合进行高分辨率X射线结构分析,其衍射分辨率优于1.5埃。纳豆球蛋白以单斜空间群P21结晶,α = 46.9埃,b = 75.5埃,c = 50.9埃,α = γ = 90°,β = 120.5°。该蛋白质由一条多肽链组成,在SDS/聚丙烯酰胺凝胶电泳后,其与豆球蛋白或豌豆球蛋白的亚基不一致,相对分子质量约为33,000。