title: 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.
authors.affiliation: The National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871, People's Republic of China.
authors.forename: Lu
authors.initials: L
authors.lastname: Lu
authors.forename: Jie
authors.initials: J
authors.lastname: Nan
authors.forename: Wei
authors.initials: W
authors.lastname: Mi
authors.forename: Chun-Hong
authors.initials: CH
authors.lastname: Wei
authors.forename: Lan-Fen
authors.initials: LF
authors.lastname: Li
authors.forename: Yi
authors.initials: Y
authors.lastname: Li
mesh_terms: D017360:Arabidopsis / Q000737:chemistry*; D029681:Arabidopsis Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D018832:Molecular Chaperones / Q000737:chemistry*
chemical_list: D029681:Arabidopsis Proteins; D018832:Molecular Chaperones; C553426:tubulin-folding cofactor A, Arabidopsis