Pal G P, Jany K D, Tsernoglou D
European Molecular Biology Laboratory, Heidelberg, Germany.
Proteins. 1994 Jun;19(2):161-2. doi: 10.1002/prot.340190210.
Crystals of a complex of proteinase K (molecular mass, 28,790 Da) with its naturally occurring protein inhibitor PK13 (19,641 Da), have been prepared by a microdialysis technique and modified by hanging drop vapor diffusion against 25% ammonium sulfate in 50 mM Tris-HCl, pH 7.8. The crystals are long prisms with diamond-shaped cross sections of 0.2 x 0.4 x 1.5 mm3 and they diffract X-rays to a resolution of 2.5 A. They belong to the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 64.1 A, b = 66.8 A, and c = 133.8 A. Assuming one whole complex in the asymmetric unit, one obtains VM = 2.95 A3/Da and the solvent content, Vsolv = 58.3%.
通过微透析技术制备了蛋白酶K(分子量28,790道尔顿)与其天然存在的蛋白抑制剂PK13(19,641道尔顿)的复合物晶体,并通过在50 mM Tris-HCl(pH 7.8)中对抗25%硫酸铵的悬滴气相扩散进行修饰。晶体为长棱柱体,菱形横截面尺寸为0.2×0.4×1.5 mm3,能将X射线衍射至2.5埃的分辨率。它们属于正交空间群P2(1)2(1)2(1),晶胞尺寸a = 64.1埃,b = 66.8埃,c = 133.8埃。假设不对称单元中有一个完整的复合物,则可得VM = 2.95埃3/道尔顿,溶剂含量Vsolv = 58.3%。