PURIFICATION AND CRYSTALLIZATION OF RECOMBINANT ESCHERICHIA-COLI MALATE-DEHYDROGENASE

被引：11

作者：

HALL, MD

LEVITT, DG

MCALLISTERHENN, L

BANASZAK, LJ

机构：

[1] UNIV MINNESOTA,DEPT BIOCHEM,MINNEAPOLIS,MN 55455

[2] UNIV MINNESOTA,DEPT PHYSIOL,MINNEAPOLIS,MN 55455

[3] UNIV CALIF IRVINE,COLL MED,DEPT BIOL CHEM,IRVINE,CA 92717

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1991年 / 220卷 / 03期

关键词：

MALATE DEHYDROGENASE; MDHASE; CITRIC ACID CYCLE; DEHYDROGENASE; MDH;

D O I：

10.1016/0022-2836(91)90099-R

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：

Malate dehydrogenase from Escherichia coli has been crystallized with polyethylene glycol and citrate buffer at pH 5·7. The enzyme was obtained from an E. coli strain in which the chromosomal malate dehydrogenase gene was contained on a pBR322 vector. Two types of crystals have been observed; a monoclinic C2 form and an orthorhombic C2221 form, which is found infrequently. Monoclinic crystals were used as seeds in several rounds of crystallization until large crystals suitable for diffraction analysis were available. A complete X-ray data set to 2·0 Å has been collected. © 1991.

引用

页码：551 / 553

页数：3

共 9 条

[1]

BERNSTEIN LH, 1978, J BIOL CHEM, V253, P8697

[2] REFINED CRYSTAL-STRUCTURE OF CYTOPLASMIC MALATE-DEHYDROGENASE AT 2.5-A RESOLUTION [J].