CRYSTALLIZATION AND PRELIMINARY-X-RAY INVESTIGATION OF LIPOXYGENASE-3 FROM SOYBEANS

被引：5

作者：

AXELROD, B ^{[1
]}

STECZKO, J

MINOR, W

STOJANOFF, V

机构：

[1] PURDUE UNIV, DEPT BIOCHEM, W LAFAYETTE, IN 47907 USA

[2] POLISH ACAD SCI, INST CATALYSIS & SURFACE CHEM, PL-32239 KRAKOW, POLAND

[3] PURDUE UNIV, DEPT BIOL SCI, W LAFAYETTE, IN 47907 USA

[4] BROOKHAVEN NATL LAB, DEPT BIOL, UPTON, NY 11973 USA

来源：

PROTEIN SCIENCE | 1995年 / 4卷 / 06期

关键词：

LIPOXYGENASE; LIPOXYGENASE CRYSTALS; L-3; PROTEIN CRYSTALS; SOYBEAN;

D O I：

10.1002/pro.5560040620

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：

Soybean lipoxygenase-3 has been crystallized by the vapor diffusion method in 16-20% polyethylene glycol (average M(r), 3,400), 0.2 M sodium acetate buffer, pH 5.7, at 21 degrees C, at a protein concentration of 8-15 mg/mL. The crystals, which diffract to 3-Angstrom spacings, belong to the monoclinic space group C2. Cell constants are a = 111.9, b = 136.4, and c = 61.6 Angstrom and beta = 95.7 degrees. The calculated value of Matthews's constant, V-m = 2.48 Angstrom(3)/kDa, is consistent with the presence of one molecule of lipoxygenase per crystallographic asymmetric unit (Z = 4).

引用

页码：1233 / 1235

页数：3

共 18 条

[1]

Axelrod B., 1981, METHODS ENZYMOLOGY, P441, DOI DOI 10.1016/0076-6879(81)71055-3

[2] THE 3-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC-ACID 15-LIPOXYGENASE [J].