Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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 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.

Please use this url to cite or link to this publication:
author
; ; ; ; and
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 Communications
volume
66
issue
Pt 8
pages
3 pages
publisher
Wiley-Blackwell
external identifiers
  • pmid:20693679
  • 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
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}},
}