The tryptophan (W)-repressor binding protein A(WrbA ) identified as an Escherichia coli stationary-phase protein was proposed as the founding member of a new family of multimeric flavodoxin-like proteins implicated in oxidativestress defense. Since WrbAis largely uncharacterized with respect to both molecular and physiological functions, the present effort is aimed at structural characterization. WrbAapoprotein was purified and used for crystallization trials at room temperature. Multicrystals of WrbAapoprotein were obtained using standard and advanced crystallization techniques. Application of additives and gelling protein for crystallization in single capillaries yielded diffractionquality single crystals. The crystals diffracted to a resolution of 2.2A ¿ at synchrotrons DESY (X13) in Hamburg (Germany), and Elletra (XRD1) in Trieste (Italy).
Wolfova, J., Grandori, R., Kozma, E., Chatterjee, N., Carey, J., Kuta Smatanova, I. (2005). Crystallization of the flavoprotein WrbA optimized by using additives and gels. JOURNAL OF CRYSTAL GROWTH, 284(3-4), 502-505 [10.1016/j.jcrysgro.2005.07.043].
Crystallization of the flavoprotein WrbA optimized by using additives and gels
GRANDORI, RITA;
2005
Abstract
The tryptophan (W)-repressor binding protein A(WrbA ) identified as an Escherichia coli stationary-phase protein was proposed as the founding member of a new family of multimeric flavodoxin-like proteins implicated in oxidativestress defense. Since WrbAis largely uncharacterized with respect to both molecular and physiological functions, the present effort is aimed at structural characterization. WrbAapoprotein was purified and used for crystallization trials at room temperature. Multicrystals of WrbAapoprotein were obtained using standard and advanced crystallization techniques. Application of additives and gelling protein for crystallization in single capillaries yielded diffractionquality single crystals. The crystals diffracted to a resolution of 2.2A ¿ at synchrotrons DESY (X13) in Hamburg (Germany), and Elletra (XRD1) in Trieste (Italy).
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
