Crystallization of the yeast elongation factor complex eEF1A-eEF1B alpha.
Crystallization of the yeast elongation factor complex eEF1A-eEF1B alpha.
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酵母延伸因子复合物 eEF1A-eEF1B α 的结晶。
DOI：
10.1107/s0907444900015559
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Nyborg,J
中科院分区：
文献类型：
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作者：
Pedersen,L;Andersen,GR;Knudsen,CR;Kinzy,TG;Nyborg,J
以聚乙二醇2000单甲醚为沉淀剂，采用坐滴气相扩散法生长了酿酒酵母延伸因子eEF1a(原EF-1α)与核苷酸交换因子eEF1Bα的C端催化片段(原EF-1β)形成的复合体。晶体的衍射率高于1.7 ä，属于P212121空间群。晶体的晶胞参数对低温保护剂的选择很敏感。用多重反常分散技术测定了61 α复合体的结构，其中3个硒蛋氨酸残基位于11 kDa的eEF1B片段中，该片段是在大肠杆菌中表达的全长eEF1B的限制性蛋白水解物。
Crystals of the Saccharomyces cerevisiae elongation factor eEF1A (formerly EF-1α) in complex with a catalytic C-terminal fragment of the nucleotide-exchange factor eEF1Bα (formerly EF-1β) were grown by the sitting-drop vapour-diffusion technique, using polyethylene glycol 2000 monomethyl ether as precipitant. Crystals diffract to better than 1.7 Å and belong to the space group P212121. The unit-cell parameters of the crystals are sensitive to the choice of cryoprotectant. The structure of the 61 kDa complex was determined with the multiple anomalous dispersion technique using three selenomethionine residues in a 11 kDa eEF1Bα fragment generated by limited proteolysis of full-length eEF1Bα expressed in Escherichia coli.