Crystallization and preliminary X-ray analysis of tubulin-folding cofactor A from Arabidopsis thaliana
(2010) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications 66(Pt 8). p.6-954- 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.
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- author
- Lu, Lu ; Nan, Jie LU ; Mi, Wei ; Wei, Chun-Hong ; Li, Lan-Fen and Li, Yi
- organization
- publishing date
- 2010-08-01
- type
- Contribution to journal
- publication status
- published
- keywords
- Arabidopsis, Arabidopsis Proteins, Crystallization, Crystallography, X-Ray, Molecular Chaperones
- in
- Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
- volume
- 66
- issue
- Pt 8
- pages
- 3 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:77955447166
- pmid:20693679
- ISSN
- 2053-230X
- DOI
- 10.1107/S1744309110023900
- language
- English
- LU publication?
- yes
- id
- 6d3686b5-08b5-43d6-8c7b-b69bf0be0ebb
- date added to LUP
- 2016-09-07 22:51:58
- date last changed
- 2024-01-04 12:05:56
@article{6d3686b5-08b5-43d6-8c7b-b69bf0be0ebb, abstract = {{<p>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.</p>}}, author = {{Lu, Lu and Nan, Jie and Mi, Wei and Wei, Chun-Hong and Li, Lan-Fen and Li, Yi}}, issn = {{2053-230X}}, keywords = {{Arabidopsis; Arabidopsis Proteins; Crystallization; Crystallography, X-Ray; Molecular Chaperones}}, language = {{eng}}, month = {{08}}, number = {{Pt 8}}, pages = {{6--954}}, publisher = {{Wiley-Blackwell}}, series = {{Acta Crystallographica. Section F: Structural Biology and Crystallization Communications}}, title = {{Crystallization and preliminary X-ray analysis of tubulin-folding cofactor A from Arabidopsis thaliana}}, url = {{http://dx.doi.org/10.1107/S1744309110023900}}, doi = {{10.1107/S1744309110023900}}, volume = {{66}}, year = {{2010}}, }