CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC ANALYSIS OF THE SOYBEAN PROGLYCININ EXPRESSED IN ESCHERICHIA-COLI

被引：17

作者：

UTSUMI, S

GIDAMIS, AB

MIKAMI, B

KITO, M

机构：

[1] Research Institute for Food Science, Kyoto University

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 233卷 / 01期

关键词：

PROGLYCININ; SOYBEAN; CRYSTALLIZATION; X-RAY ANALYSIS;

D O I：

10.1006/jmbi.1993.1495

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 P41 or P43, with unit cell dimensions of a=b=115.2 Å, and c=147.1 Å. The asymmetric unit contains three molecules of proglycinin, with crystal volume per protein mass (Vm) of 3.05 Å3/Da and solvent content of 58.4% by volume. The crystals diffract X-rays to a resolution limit of at least 2.9 Å and are resistant to X-ray radiation damage. They appear to be suitable for X-ray structure analysis. © 1993 Academic Press Limited.

引用

页码：177 / 178

页数：2

共 14 条

[1]

BARTON KA, 1982, J BIOL CHEM, V257, P6089

[2] DETERMINATION OF THE PROTEIN-CONTENT OF CRYSTALS FORMED BY MASTIGOCLADUS-LAMINOSUS C-PHYCOCYANIN, CHROOMONAS-SPEC PHYCOCYANIN-645 AND MODIFIED HUMAN-FIBRINOGEN USING AN IMPROVED FICOLL DENSITY GRADIENT-METHOD [J].