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

Tubulin‐folding cofactor A (TFC A) is a molecular post‐chaperonin that is involved in the β‐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. A...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-08, Vol.66 (8), p.954-956
Main Authors: Lu, Lu, Nan, Jie, Mi, Wei, Wei, Chun-Hong, Li, Lan-Fen, Li, Yi
Format: Article
Language:English
Subjects:
Arabidopsis
Arabidopsis - chemistry
Arabidopsis Proteins
Arabidopsis Proteins - chemistry
Cleavage
Crystallization
Crystallization Communications
Crystallography, X-Ray
Crystals
Diffraction
E coli
Escherichia coli
Homogeneity
Molecular Chaperones
Molecular Chaperones - chemistry
Organisms
Synchrotron radiation
Thrombin
tubulin-folding cofactor A
Yeasts
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Summary:Tubulin‐folding cofactor A (TFC A) is a molecular post‐chaperonin that is involved in the β‐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 Å resolution using synchrotron radiation and belonged to space group I41, with unit‐cell parameters a = 55.0, b = 55.0, c = 67.4 Å.
ISSN:1744-3091
2053-230X
1744-3091
2053-230X
DOI:10.1107/S1744309110023900