Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase

被引：13

作者：

Hansson, M

Al-Karadaghi, S

机构：

[1] LUND UNIV, DEPT MOLEC BIOPHYS, CTR CHEM, S-22100 LUND, SWEDEN

[2] LUND UNIV, DEPT MICROBIOL, S-22362 LUND, SWEDEN

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 1995年 / 23卷 / 04期

关键词：

Bacillus subtilis; ferrochelatase; X-ray diffraction; crystallization; heme synthesis;

D O I：

10.1002/prot.340230419

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：

Bacillus subtilis ferrochelatase (EC 4.99.1.1), the final enzyme in protoheme IX biosynthesis, was produced with an inducible T7 RNA polymerase expression system in Escherichia coli and purified from the soluble cell fraction. It was crystallized from polyethylene glycol solution using the microseeding technique. The crystals diffract to a minimum Bragg spacing of 2.1 Angstrom. The space group is P4(2) with unit cell dimensions a = b = 50.2 Angstrom, c = 120.1 Angstrom. (C) 1995 Wiley-Liss, Inc.

引用

页码：607 / 609

页数：3

共 16 条

[1]

ABBAS A, 1993, J BIOL CHEM, V268, P8541

[2]

Dailey H. A., 1990, BIOSYNTHESIS HEME CH, P123

[3] INTERACTION OF FREE PORPHYRINS AND METALLOPORPHYRINS WITH MOUSE FERROCHELATASE - A MODEL FOR THE ACTIVE-SITE OF FERROCHELATASE [J].