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Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin from Homo sapiens.
- Source :
- Acta Crystallographica: Section F, Structural Biology Communications; Sep2015, Vol. 71 Issue 9, p1189-1193, 5p
- Publication Year :
- 2015
-
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 P2<subscript>1</subscript>2<subscript>1</subscript>2, with unit-cell parameters a = 123.2, b = 152.4, c = 105.9 Å. [ABSTRACT FROM AUTHOR]
- Subjects :
- CRYSTALLIZATION
PROTEINS
MOLECULAR chaperones
HUMAN beings
X-ray diffraction
Subjects
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 71
- Issue :
- 9
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 109218476
- Full Text :
- https://doi.org/10.1107/S2053230X15013990