在大肠杆菌中表达的大豆前体大豆球蛋白的结晶及初步X射线晶体学分析。

Crystallization and preliminary X-ray crystallographic analysis of the soybrean proglycinin expressed in Escherichia coli.

作者信息

Utsumi S, Gidamis A B, Mikami B, Kito M

机构信息

Research Institute for Food Science, Kyoto University, Japan.

出版信息

J Mol Biol. 1993 Sep 5;233(1):177-8. doi: 10.1006/jmbi.1993.1495.

DOI:10.1006/jmbi.1993.1495

PMID:8377187

Abstract

Glycinin is one of the dominant storage proteins of soybean seeds. Soybean proglycinin expressed in Escherichia coli has been crystallized from Tris.HCl buffer (pH 7.6) by the dialysis equilibrium method. The crystals belong to the tetragonal system, space group P4(1) or P4(3), with unit cell dimensions of a = b = 115.2 A, and c = 147.1 A. The asymmetric unit contains three molecules of proglycinin, with crystal volume per protein mass (Vm) of 3.05 A3/Da and solvent content of 58.4% by volume. The crystals diffract X-rays to a resolution limit of at least 2.9 A and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis.

摘要

大豆球蛋白是大豆种子中的主要贮藏蛋白之一。在大肠杆菌中表达的大豆前体大豆球蛋白已通过透析平衡法从Tris.HCl缓冲液（pH 7.6）中结晶出来。晶体属于四方晶系，空间群为P4(1)或P4(3)，晶胞参数为a = b = 115.2 Å，c = 147.1 Å。不对称单元包含三个前体大豆球蛋白分子，每蛋白质质量的晶体体积（Vm）为3.05 Å³/Da，溶剂含量为58.4%（体积）。这些晶体的X射线衍射分辨率极限至少为2.9 Å，并且对X射线辐射损伤具有抗性。它们似乎适合进行X射线结构分析。