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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution.
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Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution.

机译:结晶的微重力下槲寄生凝集素我与腺嘌呤从槲寄生的专辑1.9一磷酸和晶体结构决议。

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摘要

The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album in complex with adenine has been refined to 1.9 A resolution. High quality crystals of the ML-I complex were obtained by the method of vapour diffusion using the high density protein crystal growth system (HDPCG) on the international space station, mission ISS 6A. Hexagonal crystals were grown during three months under microgravity conditions. Diffraction data to 1.9A were collected applying synchrotron radiation and cryo- techniques. The structure was refined subsequently to analyse the structure of ML-I and particularly the active site conformation, complexed by adenine that mimics the RNA substrate binding.
机译:ribosome-inactivating的晶体结构蛋白(RIP)槲寄生植物血凝素(ML-I)槲寄生专辑与腺嘌呤是复杂的精致到1.9一项决议。晶体ML-I复杂的得到的使用高密度蒸汽扩散的方法蛋白质晶体生长系统(HDPCG)国际空间站,空间站使命6。六角晶体生长期间三个月在微重力条件下。1.9收集应用同步辐射和低温技术。随后精炼的结构分析ML-I特别是活性部位由腺嘌呤,模仿构象,口感RNA衬底绑定。

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