Translation initiation factor 2 alpha (aIF2 alpha) and beta (aIF2 beta) subunits from archaebacteria Sulfolobus solfataricus have been crystallized here for the first time. Indeed aIF2 alpha small microcrystals of about 10-20 mu m appeared with the thin film nanotemplate method, but not with the classical hanging-drop method. Similarly, under a polarization light microscope microcrystals of larger size (up to about 50-80 mu m) of aIF2 beta were also obtained using the same procedure, but not with the classical hanging-drop method. We subsequently confirmed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectroscopy the identification of the corresponding dissolved crystals as formed by the aIF2 alpha and beta proteins.
Crystallization of alpha and beta subunits of IF2 translation initiation factor from archaebacteria Sulfolobus solfataricus / E. Pechkova, F. Vasile, R. Spera, C. Nicolini. - In: JOURNAL OF CRYSTAL GROWTH. - ISSN 0022-0248. - 310:16(2008), pp. 3767-3770. [10.1016/j.jcrysgro.2008.05.036]
Crystallization of alpha and beta subunits of IF2 translation initiation factor from archaebacteria Sulfolobus solfataricus
F. Vasile;R. Spera;
2008
Abstract
Translation initiation factor 2 alpha (aIF2 alpha) and beta (aIF2 beta) subunits from archaebacteria Sulfolobus solfataricus have been crystallized here for the first time. Indeed aIF2 alpha small microcrystals of about 10-20 mu m appeared with the thin film nanotemplate method, but not with the classical hanging-drop method. Similarly, under a polarization light microscope microcrystals of larger size (up to about 50-80 mu m) of aIF2 beta were also obtained using the same procedure, but not with the classical hanging-drop method. We subsequently confirmed by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectroscopy the identification of the corresponding dissolved crystals as formed by the aIF2 alpha and beta proteins.File | Dimensione | Formato | |
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