Journal of Crystal Growth, Vol.310, No.16, 3767-3770, 2008
Crystallization of alpha and beta subunits of IF2 translation initiation factor from archaebacteria Sulfolobus solfataricus
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. (c) 2008 Elsevier B.V. All rights reserved.
Keywords:biocrystallization;nanostructures;single crystal growth;Langmuir-Blodgett protein thin films;proteins