来自大肠杆菌的单体铜锌超氧化物歧化酶的结晶及初步X射线分析。
Crystallization and preliminary X-ray analysis of the monomeric Cu,Zn superoxide dismutase from Escherichia coli.
作者信息
Battistoni A, Folcarelli S, Rotilio G, Capasso C, Pesce A, Bolognesi M, Desideri A
机构信息
Dipartimento di Biologia, Università di Tor Vergata, Italy.
出版信息
Protein Sci. 1996 Oct;5(10):2125-7. doi: 10.1002/pro.5560051020.
The Cu,Zn superoxide dismutase (Cu,Zn SOD) originally isolated from the periplasmic space of Escherichia coli has been cloned and overexpressed in the E. coli strain BMH 71/18. The protein has been purified as a single component of 17,000 Da, corresponding to one subunit of the common dimeric eukaryotic Cu,Zn SODs. Large crystals of the purified protein have been grown in the presence of polyethylene glycol 4,000 at pH 8.5; the crystals belong to the monoclinic space group P2(1), with unit cell constants a = 33.1 A, b = 52.6 A, c = 43.3 A, beta = 111.4 degrees. One SOD subunit is contained in the asymmetric unit, yielding a Vm value of 2.1 A3/Da; the crystals diffract X-rays beyond 2.0 A resolution.
最初从大肠杆菌周质空间分离得到的铜锌超氧化物歧化酶（Cu,Zn SOD）已被克隆并在大肠杆菌菌株BMH 71/18中过量表达。该蛋白质已被纯化，为一种17,000道尔顿的单一成分，相当于常见二聚体真核铜锌超氧化物歧化酶的一个亚基。纯化后的蛋白质在pH 8.5的条件下，于聚乙二醇4000存在时生长出大晶体；这些晶体属于单斜空间群P2(1)，晶胞参数a = 33.1 Å，b = 52.6 Å，c = 43.3 Å，β = 111.4°。不对称单位中包含一个超氧化物歧化酶亚基，Vm值为2.1 ų/道尔顿；这些晶体对X射线的衍射分辨率超过2.0 Å。
Zotero 插件