Crystallization of alpha and beta subunits of IF2 translation initiation factor from archaebacteria Sulfolobus solfataricus

被引:4
|
作者
Pechkova, E. [1 ,2 ]
Vasile, F. [1 ]
Spera, R. [1 ]
Nicolini, C. [1 ,2 ]
机构
[1] Univ Genoa, Nanoworld Inst, CIRSDNNOB, I-16132 Genoa, Italy
[2] Fdn Elba, I-00187 Rome, Italy
关键词
biocrystallization; nanostructures; single crystal growth; Langmuir-Blodgett protein thin films; proteins;
D O I
10.1016/j.jcrysgro.2008.05.036
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
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.
引用
收藏
页码:3767 / 3770
页数:4
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