枯草芽孢杆菌铁螯合酶的纯化、结晶及初步X射线分析。
Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase.
作者信息
Hansson M, Al-Karadaghi S
机构信息
Department of Microbiology, Lund University, Sweden.
出版信息
Proteins. 1995 Dec;23(4):607-9. doi: 10.1002/prot.340230419.
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 A. The space group is P4(2) with unit cell dimensions a = b = 50.2 A, c = 120.1 A.
枯草芽孢杆菌亚铁螯合酶（EC 4.99.1.1）是原卟啉IX生物合成的最后一种酶，它通过大肠杆菌中的诱导型T7 RNA聚合酶表达系统产生，并从可溶性细胞组分中纯化出来。使用微量接种技术从聚乙二醇溶液中使其结晶。晶体的最小布拉格间距为2.1埃，可用于衍射分析。其空间群为P4(2)，晶胞参数为a = b = 50.2埃，c = 120.1埃。
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