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拟南芥微管蛋白折叠辅助因子A的结晶及初步X射线分析

Crystallization and preliminary X-ray analysis of tubulin-folding cofactor A from Arabidopsis thaliana.

作者信息

Lu Lu, Nan Jie, Mi Wei, Wei Chun-Hong, Li Lan-Fen, Li Yi

机构信息

The National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871, People's Republic of China.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt 8):954-6. doi: 10.1107/S1744309110023900. Epub 2010 Jul 29.

DOI:10.1107/S1744309110023900
PMID:20693679
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2917302/
Abstract

Tubulin-folding cofactor A (TFC A) is a molecular post-chaperonin that is involved in the beta-tubulin-folding pathway. It has been identified in many organisms including yeasts, humans and plants. In this work, Arabidopsis thaliana TFC A was expressed in Escherichia coli and purified to homogeneity. After thrombin cleavage, a well diffracting crystal was obtained by the sitting-drop vapour-diffusion method at 289 K. The crystal diffracted to 1.6 A resolution using synchrotron radiation and belonged to space group I4(1), with unit-cell parameters a=55.0, b=55.0, c=67.4 A.

摘要

微管蛋白折叠辅助因子A(TFC A)是一种分子伴侣后因子,参与β-微管蛋白折叠途径。它已在包括酵母、人类和植物在内的许多生物体中被鉴定出来。在这项工作中,拟南芥TFC A在大肠杆菌中表达并纯化至同质。凝血酶切割后,通过坐滴气相扩散法在289 K下获得了一颗衍射良好的晶体。该晶体利用同步辐射衍射至1.6 Å分辨率,属于空间群I4(1),晶胞参数a = 55.0,b = 55.0,c = 67.4 Å。

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