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Crystallization and...
Crystallization and preliminary X-ray analysis of tubulin-folding cofactor A from Arabidopsis thaliana
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Lu, Lu (author)
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- Nan, Jie (author)
- Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory,Peking University
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Mi, Wei (author)
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Wei, Chun-Hong (author)
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Li, Lan-Fen (author)
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Li, Yi (author)
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(creator_code:org_t)
- 2010
- 2010
- English 3 s.
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In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications. - 2053-230X. ; 66:Pt 8, s. 6-954
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http://dx.doi.org/10...
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Abstract
Subject headings
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- 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.
Keyword
- Arabidopsis
- Arabidopsis Proteins
- Crystallization
- Crystallography, X-Ray
- Molecular Chaperones
Publication and Content Type
- art (subject category)
- ref (subject category)
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