Hamiaux C, Prangé T, Riès-Kautt M, Ducruix A, Lafont S, Astier J P, Veesler S
Laboratoire pour l'Utilisation du Rayonnement Electromagnétique (LURE), Bâtiment 209d, Université Paris-Sud, 91405 Orsay CEDEX, France.
Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):103-13. doi: 10.1107/S0907444998008725. Epub 1999 Jan 1.
The structure of a monoclinic form of bovine pancreatic trypsin inhibitor (BPTI) crystallized from a thiocyanate solution has been determined and refined at 2.7 A resolution. The space group is P21 with a = 71.56, b = 73.83, c = 64.47 A, beta = 93.9 degrees and Z = 20. The ten independent molecules were located by a multi-body molecular-replacement search as developed in the AMoRe program, starting from a single monomer model (PDB code: 6PTI). The molecular arrangement of the subunits is a decamer resulting from the combination of two orthogonal fivefold and twofold non-crystallographic axes. This builds a globular micelle-like particle which minimizes hydrophobic interactions with the solvent. The refinement was conducted with non-crystallographic symmetry constraints up to a final residual of R = 0.20 (Rfree= 0.26). The root-mean-square deviations from ideal geometry were 0.015 A and 1.6 degrees on bond distances and bond angles, respectively. Several sites for thiocyanate ions were analyzed.
已确定并在2.7埃分辨率下精修了从硫氰酸盐溶液中结晶出的单斜晶型牛胰蛋白酶抑制剂（BPTI）的结构。空间群为P21，a = 71.56，b = 73.83，c = 64.47埃，β = 93.9°，Z = 20。十个独立分子通过在AMoRe程序中开发的多体分子置换搜索定位，起始于单个单体模型（PDB代码：6PTI）。亚基的分子排列是由两个正交的五重轴和二重非晶轴组合形成的十聚体。这构建了一个球状的类似胶束的颗粒，使与溶剂的疏水相互作用最小化。精修在非晶对称约束下进行，最终残余因子R = 0.20（Rfree = 0.26）。与理想几何结构的均方根偏差在键长和键角上分别为0.015埃和1.6°。分析了几个硫氰酸根离子的位点。
