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Purification, crystallization, and preliminary X‐ray analysis of Bacillus subtilis ferrochelatase
Author(s) -
Hansson Mats,
AlKaradaghi Salam
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230419
Subject(s) - bacillus subtilis , polyethylene glycol , ferrochelatase , escherichia coli , crystallization , chemistry , enzyme , t7 rna polymerase , rna polymerase , biochemistry , biology , heme , gene , bacteria , organic chemistry , bacteriophage , genetics
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 Å. The space group is P 4 2 with unit cell dimensions a = b = 50.2 Å, c = 120.1 Å. © 1995 Wiley‐Liss, Inc.