Crystallization of Hfq protein: a bacterial gene-expression regulator

Ioulia M Vassilieva; Alexey D Nikulin; Udo Blasi; Isabella Moll; Maria B Garber

doi:10.1107/s0907444903006929

Crystallization of Hfq protein: a bacterial gene-expression regulator

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

Authors

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

Affiliation

¹ Institute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.

PMID: 12777774
DOI: 10.1107/s0907444903006929

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cloning, Molecular
Crystallization
Crystallography, X-Ray
Escherichia coli / genetics*
Escherichia coli / metabolism*
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / genetics
Gene Expression Regulation, Bacterial / genetics*
Host Factor 1 Protein / chemistry*
Host Factor 1 Protein / genetics
RNA, Bacterial / biosynthesis
RNA, Bacterial / genetics

Substances

Escherichia coli Proteins
Hfq protein, E coli
Host Factor 1 Protein
RNA, Bacterial