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Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase (1995)

Hansson, Mats ; Al-Karadaghi, Salam

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 23 (1995), S. 607-609

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ISSN: 0887-3585

Keywords: Bacillus subtilis ; ferrochelatase ; X-ray diffraction ; crystallization ; heme synthesis ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: 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 P42 with unit cell dimensions a = b = 50.2 Å, c = 120.1 Å. © 1995 Wiley-Liss, Inc.

Additional Material: 1 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/prot.340230419

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