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Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli
Lapkouski M, Panjikar S, Kuta Smatanova I, Csefalvay E
Language English Country Great Britain
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from 2005 to 2013
PubMed Central
from 2005 to 2013
Europe PubMed Central
from 2005 to 2013
Medline Complete (EBSCOhost)
from 2005-01-01 to 2007-12-31
Wiley Online Library (archiv)
from 2005-01-01 to 2012-12-31
- MeSH
- Escherichia coli enzymology MeSH
- Financing, Organized MeSH
- Crystallization MeSH
- Crystallography, X-Ray methods MeSH
- Escherichia coli Proteins chemistry isolation & purification MeSH
- Deoxyribonucleases, Type I Site-Specific chemistry isolation & purification MeSH
EcoR124I is a multicomplex enzyme belonging to the type I restriction-modification system from Escherichia coli. Although EcoR124I 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 A, beta = 108.14 degrees. Native data were collected to 2.6 A resolution at the X12 beamline of EMBL Hamburg.
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- $a Institute of Physical Biology, University of South Bohemia in Ceske Budejovice, Zamek 136, CZ-373 33 Nove Hrady, Czech Republic
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- $a EcoR124I is a multicomplex enzyme belonging to the type I restriction-modification system from Escherichia coli. Although EcoR124I 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 A, beta = 108.14 degrees. Native data were collected to 2.6 A resolution at the X12 beamline of EMBL Hamburg.
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- $a Csaefalvay, Eva
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- $w MED00179506 $t Acta crystallographica. Section F, Structural biology and crystallization communications $g Roč. 63, č. 7 (2007), s. 582-585 $x 1744-3091
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