Literature DB >> 12777774

Crystallization of Hfq protein: a bacterial gene-expression regulator.

Ioulia M Vassilieva1, Alexey D Nikulin, Udo Blasi, Isabella Moll, Maria B Garber.   

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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Year:  2003        PMID: 12777774     DOI: 10.1107/s0907444903006929

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  The seed region of a small RNA drives the controlled destruction of the target mRNA by the endoribonuclease RNase E.

Authors:  Katarzyna J Bandyra; Nelly Said; Verena Pfeiffer; Maria W Górna; Jörg Vogel; Ben F Luisi
Journal:  Mol Cell       Date:  2012-08-16       Impact factor: 17.970

  1 in total

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