Katsuya Y, Hamada K, Hata Y, Tanaka N, Sato M, Katsube Y, Kakiuchi K, Miyata K
J Biochem. 1985 Oct;98(4):1139-42. doi: 10.1093/oxfordjournals.jbchem.a135364.
Preliminary X-ray studies on Serratia protease have been carried out using crystallographic and small angle scattering techniques. The enzyme has been crystallized in three different crystalline forms by microdialysis and vapor diffusion methods using 50 mM phosphate buffer, pH 6.0, at 24 degrees C. They have orthorhombic space groups: C222(1) for one form and P2(1)2(1)2(1) for the other two forms. A small angle X-ray scattering study showed that the radius of gyration and the maximal dimension of the molecule in aqueous solution are 26.6 A and 94.5 A, respectively. The molecular weight of the enzyme was determined to be 45,000-48,000 by various physical methods.
已使用晶体学和小角散射技术对粘质沙雷氏菌蛋白酶进行了初步的X射线研究。通过微透析和气相扩散法，在24摄氏度下使用50 mM磷酸盐缓冲液（pH 6.0），该酶已结晶为三种不同的晶体形式。它们具有正交晶系空间群：一种形式为C222(1)，另外两种形式为P2(1)2(1)2(1)。小角X射线散射研究表明，该分子在水溶液中的回转半径和最大尺寸分别为26.6 Å和94.5 Å。通过各种物理方法测定该酶的分子量为45,000 - 48,000。
