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Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Jul2007, Vol. 63 Issue 7, p582-585. 4p. 2 Diagrams, 1 Chart, 1 Graph. - Publication Year :
- 2007
-
Abstract
- 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 Å, β = 108.14°. Native data were collected to 2.6 Å resolution at the X12 beamline of EMBL Hamburg. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ENDONUCLEASES
*ESCHERICHIA coli
*CRYSTALLIZATION
*DNA
*HYDROLYSIS
Subjects
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 63
- Issue :
- 7
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 25654028
- Full Text :
- https://doi.org/10.1107/S174430910702622X