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. 2003 Jun;59(Pt 6):1061-3.
doi: 10.1107/s0907444903006929. Epub 2003 May 23.

Crystallization of Hfq protein: a bacterial gene-expression regulator

Ioulia M Vassilieva  1 , Alexey D Nikulin, Udo Blasi, Isabella Moll, Maria B Garber
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Crystallization of Hfq protein: a bacterial gene-expression regulator

Ioulia M Vassilieva et al. Acta Crystallogr D Biol Crystallogr. 2003 Jun.

Abstract

Hfq protein from Escherichia coli (EcoHfq) has been overproduced in E. coli, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion technique. Crystallization conditions for EcoHfq were found which yielded X-ray quality crystals. Crystals of EcoHfq and of Cd-, Hg- and Se-containing derivatives grew in two months, with unit-cell parameters a = b = 127.41, c = 170.36 A. The crystals belong to space group I4 and diffract to 2.1 A resolution. Two hexamers are predicted per asymmetric unit.

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