The molecular chaperone TF55
Open Access
- 21 March 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 341 (2-3), 152-155
- https://doi.org/10.1016/0014-5793(94)80447-8
Abstract
TF55‐like factor from Sulfolobus solfataricus was purified to homogeneity and analyzed by electron microscopy and image analysis to determine the symmetries of these particles. Three different procedures were used to analyze the electron micrographs: (1) fuzzy‐set based classification of the particles according to their rotational power spectra; (2) multivariate statistical analysis based on singular value decomposition; (3) circular harmonic analysis. Averages obtained from the three methods show unequivocally that the TF55‐like complex presents a 9‐fold symmetry.Keywords
This publication has 20 references indexed in Scilit:
- Structure of a molecular chaperone from a thermophilic archaebacteriumNature, 1993
- TCP1 ? molecular chaperonin of the cytoplasm?Current Biology, 1992
- T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosolNature, 1992
- Protein folding in the cellNature, 1992
- A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1Nature, 1991
- MOLECULAR CHAPERONESAnnual Review of Biochemistry, 1991
- Three-dimensional reconstruction of the sevenfolded form of Bacillus subtilis Gro EL chaperoninJournal of Structural Biology, 1990
- Fuzzy sets‐based classification of electron microscopy images of biological macromolecules with an application to ribosomal particlesJournal of Microscopy, 1990
- Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G‐250 and R‐250Electrophoresis, 1988
- Harmonic analysis of electron microscope images with rotational symmetryJournal of Molecular Biology, 1971