嗜热脂肪芽孢杆菌的耐热儿茶酚2,3-双加氧酶在大肠杆菌中表达后的纯化、结晶及初步X射线衍射研究。
Purification, crystallization and preliminary X-ray diffraction studies on the thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus expressed in Escherichia coli.
作者信息
Chen M Q, Yin C C, Zhang W, Mao Y M, Zhang Z H
机构信息
Research Group of Structural Biology and Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China.
出版信息
Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):446-7. doi: 10.1107/s0907444997014996.
PMID:9761924
Abstract
The thermostable catechol 2,3-dioxygenase of Bacillus stearothermophilus has been crystallized. The crystal is probably in the space group I222 with unit-cell dimensions of a = 70.87, b = 74.60 and c = 133.69 A. A native data set has been collected with a completeness of 96% at 2.22 A resolution and an Rmerge value of 0.091.
摘要
嗜热脂肪芽孢杆菌的热稳定儿茶酚2,3-双加氧酶已被结晶。该晶体可能属于空间群I222，晶胞参数为a = 70.87、b = 74.60和c = 133.69埃。已收集到一个天然数据集，在2.22埃分辨率下的完整性为96%，Rmerge值为0.091。
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