Crystallographic characterization of the membrane-binding domain of radixin

被引：11

作者：

Hamada, K

Matsui, T

Tsukita, S

Hakoshima, T

机构：

[1] Nara Inst Sci & Technol, Dept Mol Biol, Nara 6300101, Japan

[2] Kyoto Univ, Fac Med, Dept Cell Biol, Sakyo Ku, Kyoto 6068315, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷

关键词：

D O I：

10.1107/S0907444900006363

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Radixin is a protein which cross-links plasma membranes and actin filaments and thus forms membrane-associated cytoskeleton. The radixin N-terminal domain, which is responsible for membrane association, has been purified and crystallized by vapour diffusion with polyethylene glycol 6000. The crystals belong to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 96.36, c = 133.16 Angstrom, and diffract to a resolution of 3.0 Angstrom.

引用

页码：922 / 923

页数：2

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