绿豆胰蛋白酶抑制剂-猪胰蛋白酶复合物的晶体学研究

本文报道利用微量静置法培养出绿豆胰蛋白酶抑制剂-猪胰蛋白酶复合物可供X射线衍射分析的单晶体。晶体衍射分辨率2.7。晶体学参数测定结果为四方晶系,空间群1422,晶胞参数a=b=122.4(2),c=113.4(2)()。晶体密度1.20g/cm~3,溶剂含量36％,每个结晶学不对称单位含一个复合物分子。     

CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC DATA OF THE MUNG BEAN INHIBITOR

The trypsin inhibitor from mung bean has a molecular weight of 7984, consisting of two active domains and seven disulfide bonds. It belongs to the Bowman-Birk inhibitor. This inhibitor has been crystallized in two crystalline forms either by dialysis or by batch method. One is tetragonal with unit cell of symmetry P4_122(or P4_322) and dimensions a=b=49.21, c=158.07, each asymmetric unit containing three molecules. Another is orthorhombic with unit cell of symmetry P2_12_12 and dimensions a=39.65, b=57.18, c=52.02, each asymmetric unit containing two molecules.     

THE CRYSTALLOGRAPHIC STUDY OF THE COM PLEX OF THE LYS ACTIVE FRAGMENT OF THE MUNG BEAN TRYPSIN INHIBITOR WITH BOVINE TRYPSIN

The Lys fragment of mung bean trypsin inhibitor can combine with bovine trypsin to form a complex at an equal molar ratio. The single cxystals of the complex were obtained by using the micro-still-setting method and the X-ray diffraction extended to 1.8 resolution. Its space group is P2_12_12_1 wlth cell dimensions α=62.9(1), b=63.4(1) and c=69.7(2). There is one complex molecule in a crystallographic asymmetric unit.     

绿豆胰蛋白酶抑制剂晶体生长及晶体学参数测定

从绿豆中提取的胰蛋白酶抑制剂,分子量为7984,具有两个活性中心,7对二硫键,属于Bowman-Birk抑制剂类型。用透析法和静置法生长出四方双锥和斜方柱两种晶体。用X1线旋进照相法测定它们的晶胞参数。四方双锥晶体属四方晶系,空间群P4_122(或P4_322),a=b=49.21(?),c=158.07(?)。每个晶体学不对称单位包含三个分子。斜方柱晶体属正交晶系,空间群P2_12_12,a=39.65(?),b=57.18(?),c=52.02(?)。每个晶体学不对称单位包含两个分子。     

赣江沿岸植被及其生态对策

本文记叙了赣江沿岸的植被,同时提出了赣江存在的主要问题及其相应的生态对策,为赣江的治理提供科学依据。另外,对赣江的划分提出了新的观点。     

绿豆胰蛋白酶抑制剂Lys活力碎片-牛胰蛋白酶复合物的晶体学研究

本文证明绿豆胰蛋白酶抑制剂的Lys活力碎片能当量结合胰蛋白酶形成复合物。用微量静置法得到该复合物的单晶。X射线晶体学研究表明晶体衍射分辨率可达1.8(?),空间群为P2_12_12_1,晶胞参数a=62.9(1)(?),6=63.4(1)(?),c=69.7(2)(?)。每个结晶学不对称单位含有一个复合物分子。     

CRYSTALLOGRAPHIC STUDIES OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR WITH PORCINE TRYPSIN

The Bowman-Birk family inhibitor isolated from the mung bean can combine with porcine trypsin to form a complex at a molar ratio of 1:2. The single crystals of the complex, suitable for X-ray structural study, were obtained by using the micro-still-setting method. Initial crystallographic investigation showed that the crystals diffract to 2.7 resolution and belong to the tetragonal system. Its space group is 1422 with cell dimensions a=b=122.4 (2), c=113.4(2). The density of the crystal was 1.20g/cm~3 and the solvent constant was 36%. There is one complex molecule in a crystallographic asymmetric unit.