PMID:12777774
| Citation |
Vassilieva, IM, Nikulin, AD, Blasi, U, Moll, I and Garber, MB (2003) Crystallization of Hfq protein: a bacterial gene-expression regulator. Acta Crystallogr. D Biol. Crystallogr. 59:1061-3 |
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| 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. |
| Links | |
| Keywords |
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 |
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