The molecular chaperone TF55. Assessment of symmetry.
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.
Marco
S
S
Centro Nacional de Biotecnología (CSIC), Universidad Autónoma de Madrid, Spain.
Ureña
D
D
Carrascosa
J L
JL
Waldmann
T
T
Peters
J
J
Hegerl
R
R
Pfeifer
G
G
Sack-Kongehl
H
H
Baumeister
W
W
D019843:Archaeal Proteins; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D018833:Chaperonins; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D018832:Molecular Chaperones; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000648:ultrastructure; D016944:Sulfolobus / Q000737:chemistry*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011506:Proteins; C072010:TF55 protein, Sulfolobus shibatae; D018833:Chaperonins