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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray crystallographic analysis of the human CKIP-1 pleckstrin homology domain
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Crystallization and preliminary X-ray crystallographic analysis of the human CKIP-1 pleckstrin homology domain

机译：人CKIP-1 pleckstrin同源域的结晶和初步X射线晶体学分析

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摘要

The casein kinase 2 interacting protein-1 (CKIP-1) is involved in many cellular functions, including apoptosis, signalling pathways, cell growth, cytoskeleton and bone formation. Its N-terminal pleckstrin homology (PH) domain is thought to play an important role in membrane localization and controls shuttling of CKIP-1 between the plasma membrane and nucleus. In this study, the human CKIP-1 PH domain was purified but problems were encountered with nucleic acid contamination. An S84D/S86D/S88D triple mutant designed to abolish nucleic acid binding was purified and successfully crystallized. Single crystals diffracted to 1.7 angstrom resolution and belonged to space group P43212 with unit-cell parameters a = 53.0, b = 53.0, c = 113.8 angstrom, = = = 90.0 degrees.
机译：酪蛋白激酶2相互作用蛋白1（CKIP-1）参与许多细胞功能，包括细胞凋亡，信号通路，细胞生长，细胞骨架和骨形成。它的N末端pleckstrin同源性（PH）域被认为在膜定位中起重要作用，并控制CKIP-1在质膜和细胞核之间的穿梭。在该研究中，纯化了人CKIP-1 PH结构域，但是遇到了核酸污染问题。纯化并成功结晶了旨在消除核酸结合的S84D / S86D / S88D三重突变体。单晶衍射至1.7埃的分辨率，并属于P43212空间群，其晶胞参数a = 53.0，b = 53.0，c = 113.8埃，= = = 90.0度。

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