Solving the structure of Escherichia coli elongation factor Tu using a twinned data set
Solving the structure of Escherichia coli elongation factor Tu using a twinned data set
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DOI：
10.1107/s0907444906004021
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发表时间：
2006-04-01
影响因子：
2.2
通讯作者：
Jurnak, F
中科院分区：
文献类型：
--
作者：
Heffron, SE;Moeller, R;Jurnak, F
大肠杆菌延伸因子Tu-GDP（EF-Tu-GDP）在新型抑制剂的存在下结晶。唯一可以生长的晶体是外延的以及半面体孪晶的，高度镶嵌的并且衍射到3.4埃的分辨率，空间群P3（1）21，晶胞参数a = B = 69.55，c = 169.44埃，α = β = 90，γ = 120度。为了确定晶体中是否存在抑制剂，必须处理低质量的X射线衍射数据集。最终解决了三维结构，回答了最初的问题。结果还揭示了EF-Tu-GDP的一种新型二聚体堆积。
Escherichia coli elongation factor Tu-GDP (EF-Tu-GDP) was crystallized in the presence of novel inhibitors. The only crystals which could be grown were epitaxially as well as merohedrally twinned, highly mosaic and diffracted to a resolution of 3.4 angstrom in space group P3(1)21, with unit-cell parameters a = b = 69.55, c = 169.44 angstrom, alpha = beta = 90, gamma = 120 degrees. To determine whether an inhibitor was present in the crystal, a poor-quality X-ray diffraction data set had to be processed. The three-dimensional structure was ultimately solved and the original question answered. The results also reveal a new type of dimer packing for EF-Tu-GDP.