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.
Original language | English |
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Pages (from-to) | 954-6 |
Number of pages | 3 |
Journal | Acta Crystallographica. Section F: Structural Biology and Crystallization Communications |
Volume | 66 |
Issue number | Pt 8 |
DOIs | |
Publication status | Published - 2010 Aug 1 |
Free keywords
- Arabidopsis
- Arabidopsis Proteins
- Crystallization
- Crystallography, X-Ray
- Molecular Chaperones