Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14-16

被引：1
|
作者：
Aguda, Adeleke Halilu [1 ]
Sakwe, Amos Malle
Rask, Lars
Robinson, Robert Charles
机构：
[1] Uppsala Univ, Dept Med Biochem & Microbiol, Uppsala, Sweden
[2] Inst Mol & Cell Biol, Singapore, Singapore
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词：
D O I：
10.1107/S1744309107006689
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Human filamin A is a 280 kDa protein involved in actin-filament cross-linking. It is structurally divided into an actin-binding headpiece (ABD) and a rod domain containing 24 immunoglobulin-like (Ig) repeats. A fragment of human filamin A (Ig repeats 14-16) was cloned and expressed in Escherichia coli and the purified protein was crystallized in 1.6 M ammonium sulfate, 2% PEG 1000 and 100 mM HEPES pH 7.5. The crystals diffracted to 1.95 angstrom and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 angstrom, alpha = beta = gamma = 90 degrees.
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收藏
页码：291 / 293
页数：3
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