Open AccessCrystallization and preliminary X‐ray analysis of tubulin‐folding cofactor A from Arabidopsis thaliana
Author(s) -
Lu Lu,
Nan Jie,
Mi Wei,
Wei ChunHong,
Li LanFen,
Li Yi
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110023900
Subject(s) - crystallography , cofactor , arabidopsis thaliana , crystallization , protein folding , escherichia coli , arabidopsis , cleavage (geology) , chaperone (clinical) , biology , chemistry , biochemistry , biophysics , stereochemistry , enzyme , organic chemistry , paleontology , fracture (geology) , gene , mutant , medicine , pathology
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 I 4 1 , with unit‐cell parameters a = 55.0, b = 55.0, c = 67.4 Å.