TY - JOUR
T1 - Crystallization of the flavoprotein WrbA optimized by using additives and gels
AU - Wolfova, Julie
AU - Grandori, Rita
AU - Kozma, Erika
AU - Chatterjee, Neal
AU - Carey, Jannette
AU - Smatanova, Ivana Kuta
N1 - Funding Information:
This work is supported by grant of the Ministry of Education of the CR (KONTAKT ME640) to I.K.S. and by NSF Grant INT-03-09049 to J.C. Grants MSM6007665808 and AVOZ60870520 are also acknowledged. Thanks to Jeroen Mesters and Maurizio Polentarutti for their help with diffraction measurements of WrbA apoprotein crystals.
PY - 2005/11/1
Y1 - 2005/11/1
N2 - 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 oxidative-stress defense. Since WrbA is largely uncharacterized with respect to both molecular and physiological functions, the present effort is aimed at structural characterization. WrbA apoprotein was purified and used for crystallization trials at room temperature. Multicrystals of WrbA apoprotein were obtained using standard and advanced crystallization techniques. Application of additives and gelling protein for crystallization in single capillaries yielded diffraction-quality single crystals. The crystals diffracted to a resolution of 2.2 Å at synchrotrons DESY (X13) in Hamburg (Germany), and Elletra (XRD1) in Trieste (Italy).
AB - 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 oxidative-stress defense. Since WrbA is largely uncharacterized with respect to both molecular and physiological functions, the present effort is aimed at structural characterization. WrbA apoprotein was purified and used for crystallization trials at room temperature. Multicrystals of WrbA apoprotein were obtained using standard and advanced crystallization techniques. Application of additives and gelling protein for crystallization in single capillaries yielded diffraction-quality single crystals. The crystals diffracted to a resolution of 2.2 Å at synchrotrons DESY (X13) in Hamburg (Germany), and Elletra (XRD1) in Trieste (Italy).
KW - A1. Biocrystallization
KW - A1. Optimization of crystallization
KW - A2. Single crystal growth
KW - B1. Additives
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U2 - 10.1016/j.jcrysgro.2005.07.043
DO - 10.1016/j.jcrysgro.2005.07.043
M3 - Article
AN - SCOPUS:26044469866
SN - 0022-0248
VL - 284
SP - 502
EP - 505
JO - Journal of Crystal Growth
JF - Journal of Crystal Growth
IS - 3-4
ER -