Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin from Homo sapiens.

Abstract

Proper protein folding is an essential process for all organisms. Prefoldin (PFD) is a molecular chaperone that assists protein folding by delivering non-native proteins to group II chaperonin. A heterohexamer of eukaryotic PFD has been shown to specifically recognize and deliver non-native actin and tubulin to chaperonin-containing TCP-1 (CCT), but the mechanism of specific recognition is still unclear. To determine its crystal structure, recombinant human PFD was reconstituted, purified and crystallized. X-ray diffraction data were collected to 4.7 Å resolution. The crystals belonged to space group P21212, with unit-cell parameters a = 123.2, b = 152.4, c = 105.9 Å.

DOI: 10.1107/S2053230X15013990

Cite this paper

@article{Aikawa2015ExpressionPC, title={Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin from Homo sapiens.}, author={Yoshiki Aikawa and Hiroshi Kida and Yuichi Nishitani and Kunio Miki}, journal={Acta crystallographica. Section F, Structural biology communications}, year={2015}, volume={71 Pt 9}, pages={1189-93} }