Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin from Homo sapiens
- PMID: 26323306
- PMCID: PMC4555927
- DOI: 10.1107/S2053230X15013990
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.
Keywords: molecular chaperone; prefoldin; protein folding.
Figures
![Figure 1](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61ca/4555927/7c1440cc3c43/f-71-01189-fig1.gif)
![Figure 2](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61ca/4555927/ed2af2ed0e2e/f-71-01189-fig2.gif)
![Figure 3](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/61ca/4555927/55619c2bedca/f-71-01189-fig3.gif)
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