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

被引：5

作者：

Ekström, F

Stier, G

Sauer, UH ^{[1
]}

机构：

[1] Umea Univ, UCMP, Umea Ctr Mol Pathogenisis, SE-90187 Umea, Sweden

[2] EMBL, D-69017 Heidelberg, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903002063

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

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 Angstrom, beta=109.2degrees. A complete native data set from a native crystal was collected extending to 2.0 Angstrom resolution and a single-wavelength anomalous dispersion (SAD) data set to 2.9 Angstrom 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.

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页码：724 / 726

页数：3

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