Crystallization of Hfq protein: a bacterial gene-expression regulator.
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.
Vassilieva
Ioulia M
IM
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.
Nikulin
Alexey D
AD
Blasi
Udo
U
Moll
Isabella
I
Garber
Maria B
MB
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics*; D035001:Host Factor 1 Protein / Q000737:chemistry* / Q000235:genetics; D012329:RNA, Bacterial / Q000096:biosynthesis / Q000235:genetics
D029968:Escherichia coli Proteins; C087373:Hfq protein, E coli; D035001:Host Factor 1 Protein; D012329:RNA, Bacterial