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

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|66|8|954-956

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.66, Iss.8, 2010-08, pp. : 954-956

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Abstract

Tubulin‐folding cofactor A (TFC A) is a molecular post‐chaperonin that is involved in the β‐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 Å resolution using synchrotron radiation and belonged to space group I41, with unit‐cell parameters a = 55.0, b = 55.0, c = 67.4 Å.