Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone oxidoreductase from Escherichia coli.
Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone oxidoreductase from Escherichia coli.
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利用合理筛选和电子显微镜优化大肠杆菌琥珀酸：泛醌氧化还原酶的结晶。
DOI：
10.1107/s0907444903002075
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Iwata,So
中科院分区：
文献类型：
--
作者：
Horsefield,Rob;Yankovskaya,Victoria;Törnroth,Susanna;Luna-Chavez,César;Stambouli,Elizabeth;Barber,James;Byrne,Bernadette;Cecchini,Gary;Iwata,So
膜结合呼吸复合物II，琥珀酸：泛醌氧化还原酶（SQR）从大肠杆菌，已厌氧表达，然后纯化和结晶。所获得的初始晶体小且衍射差。为了便于结构测定，采用电子显微镜进行了合理筛选和样品质量分析。大肠杆菌SQR晶体属于三角空间群R32，晶胞参数a = B = 138.7，c = 521.9 μ m，λ = 2.6 μ m。 用于获得良好衍射SQR晶体的优化策略适用于广泛的膜蛋白。
The membrane-bound respiratory complex II, succinate:ubiquinone oxidoreductase (SQR) from Escherichia coli, has been anaerobically expressed, then purified and crystallized. The initial crystals obtained were small and diffracted poorly. In order to facilitate structure determination, rational screening and sample-quality analysis using electron microscopy was implemented. The crystals of SQR from E. coli belong to the trigonal space group R32, with unit-cell parameters a = b = 138.7, c = 521.9 Å, and diffract to 2.6 Å resolution. The optimization strategy used for obtaining well diffracting SQR crystals is applicable to a wide range of membrane proteins.
大肠杆菌富马酸还原酶突变体的分离及性质
影响因子：
3.2
作者：
M. Spencer;J. Guest
通讯作者：
J. Guest
大肠杆菌膜结合富马酸还原酶的过表达、纯化和结晶。
DOI：
10.1006/prep.2000.1238
发表时间：
2000
期刊：
Protein expression and purification.
影响因子：
--
作者：
Luna-Chavez,C;Iverson,TM;Rees,DC;Cecchini,G
通讯作者：
Cecchini,G
大肠杆菌琥珀酸：泛醌氧化还原酶的纯化、结晶和初步晶体学研究。
DOI：
10.1016/s0005-2728(01)00236-5
发表时间：
2002
期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
Törnroth,Susanna;Yankovskaya,Victoria;Cecchini,Gary;Iwata,So
通讯作者：
Iwata,So