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

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.

SUBMITTER: Lu L

PROVIDER: S-EPMC2917302 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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

Lu Lu L Nan Jie J Mi Wei W Wei Chun-Hong CH Li Lan-Fen LF Li Yi Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20100729 Pt 8

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 belo ...[more]

PMID: 20693679

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