Crystallization and preliminary characterization of crystals of the C-terminal half fragment of tropomodulin

被引：8

作者：

Krieger, I ^{[1
]}

Kostyukova, AS ^{[1
]}

Maéda, Y ^{[1
]}

机构：

[1] RIKEN, Harima Inst Spring 8, Lab Struct Biochem, Sayo, Hyogo 6795148, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444901003924

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Tropomodulin (40 kDa) stabilizes the actin-tropomyosin filament by capping the P end (slow-growing end). The C-terminal half (C20, 20 kDa), an independently folded domain that is believed to be responsible for the P-end capping, has been crystallized. Crystals grew in the presence of Zn2+ as the solution pH was increased from 3 towards the pI of the protein. The crystals belong to the trigonal space group R3. They have unit-cell parameters a = b = 69.6, c = 101.3 Angstrom (mean values, with a estimated standard deviation of 0.009 Angstrom) and diffract to 1.9 Angstrom resolution when the frozen crystals were measured at 120 K on a rotating-anode X-ray source at 120 K.

引用

页码：743 / 744

页数：2

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