Crystallization and diffracton to ultrahigh resolution (0.8 A) of a designed variant of the Rop protein

Aspasia Spyridaki; Nicholas M. Glykos; Dina KotsifakiVasiliki E. FadouloglouMichael Kokkinidis

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Crystallization and diffracton to ultrahigh resolution (0.8 A) of a designed variant of the Rop protein

机译：结晶和diffracton超高决议(0.8)的设计变量蛋白质绳

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摘要

The Rop protein is the paradigm of a highly regular four-α-helix bundle and as such has been subject to numerous structural and mutagenesis studies. Crystals of a designed Rop variant which establishes a continuous heptad pattern through the bend region have been obtained by a combination of vapour-diffusion and seeding techniques. The crystals diffract to ultrahigh (0.8 A) resolution using synchrotron radiation and cryogenic conditions.

机译：罗普蛋白是一个高度的范式常规四个α螺旋束,因此许多结构和诱变研究。通过建立一个连续七个模式弯曲地区已经取得的vapour-diffusion和播种技术。使用同步辐射(0.8)的决议和低温条件。

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《Acta crystallographica.Section D. Biological crystallography》 |2000年第8期|1015-1016|共2页
作者
Aspasia Spyridaki; Nicholas M. Glykos; Dina KotsifakiVasiliki E. FadouloglouMichael Kokkinidis;
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Institute of Molecular Biology and Biotechnology (IMBB), PO Box 1527, GR-71110 Heraklion, Crete, Greece;

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正文语种英语
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Mutagenesis; crystals; Resolving powersynchrotron radiationProteinseed inoculationCrystallization;

机译：诱变;晶体;解决powersynchrotronradiationProteinseed inoculationCrystallization;

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Crystallization and diffracton to ultrahigh resolution (0.8 A) of a designed variant of the Rop protein

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