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

来源：

JOURNAL OF CRYSTAL GROWTH | 2008年 / 310卷 / 16期

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

页码：3767 / 3770

页数：4