Crystallization of the actin-binding domain of human alpha-actinin: analysis of microcrystals of SeMet-labelled protein.

Ekstrom F; Stier G; Sauer UH

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Crystallization of the actin-binding domain of human alpha-actinin: analysis of microcrystals of SeMet-labelled protein.

机译：actin-binding域的结晶人类alpha-actinin:分析的微晶核SeMet-labelled蛋白质。

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摘要

alpha-Actinin forms antiparallel homodimers that cross-link actin filaments from adjacent sarcomeres within the Z-discs of striated muscle. The N-terminal actin-binding domain (ABD) is composed of two calponin homology (CH) domains followed by four spectrin-like repeats and a calmodulin-like EF-hand domain at the C-terminus. The ABD of human alpha-actinin crystallizes in space group P2(1), with unit-cell parameters a = 101.9, b = 38.4, c = 154.9 A, beta = 109.2 degrees. A complete native data set from a native crystal was collected extending to 2.0 A resolution and a single-wavelength anomalous dispersion (SAD) data set to 2.9 A resolution was collected from a selenomethionine-labelled microcrystal using the microfocusing beamline ID-13 at the ESRF. Analysis of the anomalous contribution shows a rapid decrease in the sigma(normal)/sigma(anomal) ratio owing to radiation damage.

机译：alpha-Actinin反平行的形式为从相邻交叉结合肌动蛋白丝观察在Z-discs横纹肌。氨基actin-binding域(ABD)由两个calponin同源性(CH)域四个spectrin-like重复和一个紧随其后在糖基calmodulin-like类ef - hand域。人类alpha-actinin ABD的结晶空间群P2(1),晶胞参数=101.9, b = 38.4, c = 154.9,β= 109.2度。水晶收集扩展到2.0分辨率和单波长反常色散(SAD)数据集到2.9一个决议收集从selenomethionine-labelled微晶使用微焦点beamlineID-13 ESRF。贡献了一个快速下降σ(正常)/σ(anomal)由于比例辐射损伤。

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《Acta crystallographica.Section D. Biological crystallography》 |2003年第4期|724-726|共3页
作者
Ekstrom F; Stier G; Sauer UH;
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正文语种英语
中图分类化学;
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microcrystals; alpha-Actinin; Actin CytoskeletonEF Hand MotifsRadiation InjuriesActinsAntiparallelCrystallization;

机译：microcrystals alpha-Actinin;动蛋白CytoskeletonEF手MotifsRadiationInjuriesActinsAntiparallelCrystallization;

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Crystallization of the actin-binding domain of human alpha-actinin: analysis of microcrystals of SeMet-labelled protein.

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