CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF CURCULIN - A NEW-TYPE OF SWEET PROTEIN HAVING TASTE-MODIFYING ACTION

被引：22

作者：

HARADA, S ^{[1
]}

OTANI, H ^{[1
]}

MAEDA, S ^{[1
]}

KAI, Y ^{[1
]}

KASAI, N ^{[1
]}

KURIHARA, Y ^{[1
]}

机构：

[1] YOKOHAMA NATL UNIV, FAC EDUC, DEPT CHEM, YOKOHAMA, KANAGAWA 240, JAPAN

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 238卷 / 02期

关键词：

CURCULIN; SWEET PROTEIN; TASTE-MODIFYING PROTEIN; CRYSTALLIZATION; X-RAY CRYSTALLOGRAPHY;

D O I：

10.1006/jmbi.1994.1289

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：

A taste-modifying protein, curculin, has been crystallized by the vapor diffusion method using polyethylene glycol 400 as a precipitant. The crystals belong to orthorhombic space group P212121 with unit cell dimensions: a =105 Å, b = 271 Å, c = 48·7 Å. The crystals diffract X-rays to at least a resolution of 3·0 Å and are suitable for X-ray crystallographic studies. © 1994 Academic Press, Inc.

引用

页码：286 / 287

页数：2

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