Open AccessPurification, crystallization and preliminary X‐ray analysis of the HsdR subunit of the Eco R124I endonuclease from Escherichia coli
Author(s) -
Lapkouski Mikalai,
Panjikar Santosh,
Kuta Smatanova Ivana,
Csefalvay Eva
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910702622x
Subject(s) - protein subunit , escherichia coli , endonuclease , crystallization , crystallography , chemistry , biology , genetics , dna , gene , organic chemistry
Eco R124I is a multicomplex enzyme belonging to the type I restriction‐modification system from Escherichia coli . Although Eco R124I has been extensively characterized biochemically, there is no direct structural information available about particular subunits. HsdR is a motor subunit that is responsible for ATP hydrolysis, DNA translocation and cleavage of the DNA substrate recognized by the complex. Recombinant HsdR subunit was crystallized using the sitting‐drop vapour‐diffusion method. Crystals belong to the primitive monoclinic space group, with unit‐cell parameters a = 85.75, b = 124.71, c = 128.37 Å, β = 108.14°. Native data were collected to 2.6 Å resolution at the X12 beamline of EMBL Hamburg.