Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
17620716
PubMed Central
PMC2335136
DOI
10.1107/s174430910702622x
PII: S174430910702622X
Knihovny.cz E-zdroje
- MeSH
- Escherichia coli enzymologie 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
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- endodeoxyribonuclease EcoR124I MeSH Prohlížeč
- HsdR protein, E coli MeSH Prohlížeč
- proteiny z Escherichia coli MeSH
- restrikční endonukleasy typu I 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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