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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
Jazyk angličtina Země Velká Británie
NLK
Free Medical Journals
od 2005 do 2013
PubMed Central
od 2005 do 2013
Europe PubMed Central
od 2005 do 2013
Medline Complete (EBSCOhost)
od 2005-01-01 do 2007-12-31
Wiley Online Library (archiv)
od 2005-01-01 do 2012-12-31
- MeSH
- Escherichia coli enzymologie MeSH
- financování organizované MeSH
- krystalizace MeSH
- krystalografie rentgenová metody MeSH
- proteiny z Escherichia coli chemie izolace a purifikace MeSH
- restrikční endonukleasy typu I chemie izolace a purifikace 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 Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli / $c Lapkouski M, Panjikar S, Kuta Smatanova I, Csefalvay E
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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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