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

Lu, Lu; Nan, Jie LU ; Mi, Wei; Wei, Chun-Hong; Li, Lan-Fen and Li, Yi (2010) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00 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
organization
publishing date
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 Communications2005-01-01+01:002014-01-01+01:00
volume
66
issue
Pt 8
pages
3 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:77955447166
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
2018-05-29 09:53:56
@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},
  keyword      = {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 Communications2005-01-01+01:002014-01-01+01:00},
  title        = {Crystallization and preliminary X-ray analysis of tubulin-folding cofactor A from Arabidopsis thaliana},
  url          = {http://dx.doi.org/10.1107/S1744309110023900},
  volume       = {66},
  year         = {2010},
}