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.
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
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